Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin
Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmod...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1982 |
|---|
| Umfang: |
7 Ill. 13 |
|---|
| Reproduktion: |
Wiley InterScience Backfile Collection 1832-2000 |
|---|---|
| Übergeordnetes Werk: |
in: Journal of Cellular Biochemistry - New York, N.Y. : Alan R. Liss, Inc, 19(1982) vom: Jan., Seite 45-57 |
| Übergeordnetes Werk: |
volume:19 ; year:1982 ; month:01 ; pages:45-57 ; extent:13 |
| Links: |
|---|
| Katalog-ID: |
NLEJ159843014 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ159843014 | ||
| 003 | DE-627 | ||
| 005 | 20210707020440.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070201s1982 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ159843014 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 0 | |a Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| 264 | 1 | |c 1982 | |
| 300 | |b 7 Ill. | ||
| 300 | |a 13 | ||
| 336 | |a nicht spezifiziert |b zzz |2 rdacontent | ||
| 337 | |a nicht spezifiziert |b z |2 rdamedia | ||
| 338 | |a nicht spezifiziert |b zu |2 rdacarrier | ||
| 520 | |a Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. | ||
| 533 | |f Wiley InterScience Backfile Collection 1832-2000 | ||
| 700 | 1 | |a Blum, Jacob J. |4 oth | |
| 700 | 1 | |a Hayes, A. |4 oth | |
| 700 | 1 | |a Vanaman, T. |4 oth | |
| 700 | 1 | |a Schachat, F. H. |4 oth | |
| 773 | 0 | 8 | |i in |t Journal of Cellular Biochemistry |d New York, N.Y. : Alan R. Liss, Inc |g 19(1982) vom: Jan., Seite 45-57 |w (DE-627)NLEJ159070694 |w (DE-600)1479976-5 |x 0730-2312 |7 nnns |
| 773 | 1 | 8 | |g volume:19 |g year:1982 |g month:01 |g pages:45-57 |g extent:13 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1002/jcb.240190105 |q text/html |z Deutschlandweit zugänglich |
| 912 | |a GBV_USEFLAG_U | ||
| 912 | |a ZDB-1-WIS | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 19 |j 1982 |c 1 |h 45-57 |g 13 | ||
| matchkey_str |
article:07302312:1982----::eeoeeto1sn3syentaeciiisihepcta |
|---|---|
| hierarchy_sort_str |
1982 |
| publishDate |
1982 |
| allfields |
(DE-627)NLEJ159843014 DE-627 ger DE-627 rakwb eng Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin 1982 7 Ill. 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. Wiley InterScience Backfile Collection 1832-2000 Blum, Jacob J. oth Hayes, A. oth Vanaman, T. oth Schachat, F. H. oth in Journal of Cellular Biochemistry New York, N.Y. : Alan R. Liss, Inc 19(1982) vom: Jan., Seite 45-57 (DE-627)NLEJ159070694 (DE-600)1479976-5 0730-2312 nnns volume:19 year:1982 month:01 pages:45-57 extent:13 http://dx.doi.org/10.1002/jcb.240190105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 19 1982 1 45-57 13 |
| spelling |
(DE-627)NLEJ159843014 DE-627 ger DE-627 rakwb eng Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin 1982 7 Ill. 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. Wiley InterScience Backfile Collection 1832-2000 Blum, Jacob J. oth Hayes, A. oth Vanaman, T. oth Schachat, F. H. oth in Journal of Cellular Biochemistry New York, N.Y. : Alan R. Liss, Inc 19(1982) vom: Jan., Seite 45-57 (DE-627)NLEJ159070694 (DE-600)1479976-5 0730-2312 nnns volume:19 year:1982 month:01 pages:45-57 extent:13 http://dx.doi.org/10.1002/jcb.240190105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 19 1982 1 45-57 13 |
| allfields_unstemmed |
(DE-627)NLEJ159843014 DE-627 ger DE-627 rakwb eng Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin 1982 7 Ill. 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. Wiley InterScience Backfile Collection 1832-2000 Blum, Jacob J. oth Hayes, A. oth Vanaman, T. oth Schachat, F. H. oth in Journal of Cellular Biochemistry New York, N.Y. : Alan R. Liss, Inc 19(1982) vom: Jan., Seite 45-57 (DE-627)NLEJ159070694 (DE-600)1479976-5 0730-2312 nnns volume:19 year:1982 month:01 pages:45-57 extent:13 http://dx.doi.org/10.1002/jcb.240190105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 19 1982 1 45-57 13 |
| allfieldsGer |
(DE-627)NLEJ159843014 DE-627 ger DE-627 rakwb eng Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin 1982 7 Ill. 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. Wiley InterScience Backfile Collection 1832-2000 Blum, Jacob J. oth Hayes, A. oth Vanaman, T. oth Schachat, F. H. oth in Journal of Cellular Biochemistry New York, N.Y. : Alan R. Liss, Inc 19(1982) vom: Jan., Seite 45-57 (DE-627)NLEJ159070694 (DE-600)1479976-5 0730-2312 nnns volume:19 year:1982 month:01 pages:45-57 extent:13 http://dx.doi.org/10.1002/jcb.240190105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 19 1982 1 45-57 13 |
| allfieldsSound |
(DE-627)NLEJ159843014 DE-627 ger DE-627 rakwb eng Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin 1982 7 Ill. 13 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. Wiley InterScience Backfile Collection 1832-2000 Blum, Jacob J. oth Hayes, A. oth Vanaman, T. oth Schachat, F. H. oth in Journal of Cellular Biochemistry New York, N.Y. : Alan R. Liss, Inc 19(1982) vom: Jan., Seite 45-57 (DE-627)NLEJ159070694 (DE-600)1479976-5 0730-2312 nnns volume:19 year:1982 month:01 pages:45-57 extent:13 http://dx.doi.org/10.1002/jcb.240190105 text/html Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE AR 19 1982 1 45-57 13 |
| language |
English |
| source |
in Journal of Cellular Biochemistry 19(1982) vom: Jan., Seite 45-57 volume:19 year:1982 month:01 pages:45-57 extent:13 |
| sourceStr |
in Journal of Cellular Biochemistry 19(1982) vom: Jan., Seite 45-57 volume:19 year:1982 month:01 pages:45-57 extent:13 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Journal of Cellular Biochemistry |
| authorswithroles_txt_mv |
Blum, Jacob J. @@oth@@ Hayes, A. @@oth@@ Vanaman, T. @@oth@@ Schachat, F. H. @@oth@@ |
| publishDateDaySort_date |
1982-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ159070694 |
| id |
NLEJ159843014 |
| language_de |
englisch |
| fullrecord |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ159843014</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707020440.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070201s1982 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ159843014</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1982</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="b">7 Ill.</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">13</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Wiley InterScience Backfile Collection 1832-2000</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Blum, Jacob J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hayes, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Vanaman, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Schachat, F. H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Cellular Biochemistry</subfield><subfield code="d">New York, N.Y. : Alan R. Liss, Inc</subfield><subfield code="g">19(1982) vom: Jan., Seite 45-57</subfield><subfield code="w">(DE-627)NLEJ159070694</subfield><subfield code="w">(DE-600)1479976-5</subfield><subfield code="x">0730-2312</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:19</subfield><subfield code="g">year:1982</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:45-57</subfield><subfield code="g">extent:13</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1002/jcb.240190105</subfield><subfield code="q">text/html</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-WIS</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">19</subfield><subfield code="j">1982</subfield><subfield code="c">1</subfield><subfield code="h">45-57</subfield><subfield code="g">13</subfield></datafield></record></collection>
|
| series2 |
Wiley InterScience Backfile Collection 1832-2000 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ159070694 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Illustrated |
| issn |
0730-2312 |
| topic_title |
Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
j j b jj jjb a h ah t v tv f h s fh fhs |
| hierarchy_parent_title |
Journal of Cellular Biochemistry |
| hierarchy_parent_id |
NLEJ159070694 |
| hierarchy_top_title |
Journal of Cellular Biochemistry |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ159070694 (DE-600)1479976-5 |
| title |
Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| spellingShingle |
Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| ctrlnum |
(DE-627)NLEJ159843014 |
| title_full |
Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| journal |
Journal of Cellular Biochemistry |
| journalStr |
Journal of Cellular Biochemistry |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1982 |
| contenttype_str_mv |
zzz |
| container_start_page |
45 |
| container_volume |
19 |
| physical |
7 Ill. 13 |
| format_se |
Elektronische Aufsätze |
| title_sort |
heterogeneity of 14s and 30s dynein atpase activities with respect to activation by calmodulin |
| title_auth |
Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| abstract |
Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. |
| abstractGer |
Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. |
| abstract_unstemmed |
Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin. |
| collection_details |
GBV_USEFLAG_U ZDB-1-WIS GBV_NL_ARTICLE |
| title_short |
Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin |
| url |
http://dx.doi.org/10.1002/jcb.240190105 |
| remote_bool |
true |
| author2 |
Blum, Jacob J. Hayes, A. Vanaman, T. Schachat, F. H. |
| author2Str |
Blum, Jacob J. Hayes, A. Vanaman, T. Schachat, F. H. |
| ppnlink |
NLEJ159070694 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth |
| up_date |
2024-07-05T22:48:16.586Z |
| _version_ |
1803781088572604416 |
| fullrecord_marcxml |
<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ159843014</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707020440.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070201s1982 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ159843014</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Heterogeneity of 14S and 30S dynein ATPase activities with respect to activation by calmodulin</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1982</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="b">7 Ill.</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">13</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Demembranated cilia of Tetrahymena pyriformis were extracted with KCl or Tris-EDTA and the crude dyneins from each resolved by sucrose density gradient sedimentation into 14S-K, 30S-K, 14S-E and 30S-E dyneins, respectively. The calmodulin activation ratio (ATPase activity in presence of added calmodulin/ATPase activity in absence of added calmodulin) did not vary across the 30S dynein fractions regardless of the method of extraction nor did it vary across the 14S-E region. However, in going from the “heavy” fractions to the “light” fractions of the 14S-K region, it increased markedly.The concentration of calmodulin required for half-maximal activation did not differ appreciably in the “light” versus the “heavy” fractions of the 14S-K region, suggesting that the affinity for calmodulin does not vary in these fractions. SDS-polyacrylamide gel electrophoresis studies showed the presence of several polypeptides that varied in a systematic fashion across the 14S-K region and hence may be involved in regulating the sensitivity of 14S-K dynein ATPase activity to added calmodulin.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Wiley InterScience Backfile Collection 1832-2000</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Blum, Jacob J.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Hayes, A.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Vanaman, T.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Schachat, F. H.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Journal of Cellular Biochemistry</subfield><subfield code="d">New York, N.Y. : Alan R. Liss, Inc</subfield><subfield code="g">19(1982) vom: Jan., Seite 45-57</subfield><subfield code="w">(DE-627)NLEJ159070694</subfield><subfield code="w">(DE-600)1479976-5</subfield><subfield code="x">0730-2312</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:19</subfield><subfield code="g">year:1982</subfield><subfield code="g">month:01</subfield><subfield code="g">pages:45-57</subfield><subfield code="g">extent:13</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1002/jcb.240190105</subfield><subfield code="q">text/html</subfield><subfield code="z">Deutschlandweit zugänglich</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-WIS</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">19</subfield><subfield code="j">1982</subfield><subfield code="c">1</subfield><subfield code="h">45-57</subfield><subfield code="g">13</subfield></datafield></record></collection>
|
| score |
7.4007597 |