A deletion mutation in glucosephosphate isomerase (GPI denton)
A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is t...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
|---|
| Format: |
E-Artikel |
|---|---|
| Sprache: |
Englisch |
| Erschienen: |
1979 |
|---|
| Reproduktion: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
|---|---|
| Übergeordnetes Werk: |
in: Clinica Chimica Acta - Amsterdam : Elsevier, 92(1979), 3, Seite 481-489 |
| Übergeordnetes Werk: |
volume:92 ; year:1979 ; number:3 ; pages:481-489 |
| Links: |
|---|
| Katalog-ID: |
NLEJ186301448 |
|---|
| LEADER | 01000caa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLEJ186301448 | ||
| 003 | DE-627 | ||
| 005 | 20210707042332.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 070506s1979 xx |||||o 00| ||eng c | ||
| 035 | |a (DE-627)NLEJ186301448 | ||
| 035 | |a (DE-599)GBVNLZ186301448 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 245 | 1 | 2 | |a A deletion mutation in glucosephosphate isomerase (GPI denton) |
| 264 | 1 | |c 1979 | |
| 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 A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. | ||
| 533 | |f Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 | ||
| 700 | 1 | |a Yuan, P.M. |4 oth | |
| 700 | 1 | |a Zaun, M.R. |4 oth | |
| 700 | 1 | |a Kester, M.V. |4 oth | |
| 700 | 1 | |a Snider, C.E. |4 oth | |
| 700 | 1 | |a Johnson, M. |4 oth | |
| 700 | 1 | |a Gracy, R.W. |4 oth | |
| 773 | 0 | 8 | |i in |t Clinica Chimica Acta |d Amsterdam : Elsevier |g 92(1979), 3, Seite 481-489 |w (DE-627)NLEJ184917921 |w (DE-600)1499920-1 |x 0009-8981 |7 nnns |
| 773 | 1 | 8 | |g volume:92 |g year:1979 |g number:3 |g pages:481-489 |
| 856 | 4 | 0 | |u http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 |
| 912 | |a GBV_USEFLAG_H | ||
| 912 | |a ZDB-1-SDJ | ||
| 912 | |a GBV_NL_ARTICLE | ||
| 951 | |a AR | ||
| 952 | |d 92 |j 1979 |e 3 |h 481-489 | ||
| matchkey_str |
article:00098981:1979----::dltomttoiguoehshtio |
|---|---|
| hierarchy_sort_str |
1979 |
| publishDate |
1979 |
| allfields |
(DE-627)NLEJ186301448 (DE-599)GBVNLZ186301448 DE-627 ger DE-627 rakwb eng A deletion mutation in glucosephosphate isomerase (GPI denton) 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Yuan, P.M. oth Zaun, M.R. oth Kester, M.V. oth Snider, C.E. oth Johnson, M. oth Gracy, R.W. oth in Clinica Chimica Acta Amsterdam : Elsevier 92(1979), 3, Seite 481-489 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:92 year:1979 number:3 pages:481-489 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 92 1979 3 481-489 |
| spelling |
(DE-627)NLEJ186301448 (DE-599)GBVNLZ186301448 DE-627 ger DE-627 rakwb eng A deletion mutation in glucosephosphate isomerase (GPI denton) 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Yuan, P.M. oth Zaun, M.R. oth Kester, M.V. oth Snider, C.E. oth Johnson, M. oth Gracy, R.W. oth in Clinica Chimica Acta Amsterdam : Elsevier 92(1979), 3, Seite 481-489 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:92 year:1979 number:3 pages:481-489 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 92 1979 3 481-489 |
| allfields_unstemmed |
(DE-627)NLEJ186301448 (DE-599)GBVNLZ186301448 DE-627 ger DE-627 rakwb eng A deletion mutation in glucosephosphate isomerase (GPI denton) 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Yuan, P.M. oth Zaun, M.R. oth Kester, M.V. oth Snider, C.E. oth Johnson, M. oth Gracy, R.W. oth in Clinica Chimica Acta Amsterdam : Elsevier 92(1979), 3, Seite 481-489 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:92 year:1979 number:3 pages:481-489 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 92 1979 3 481-489 |
| allfieldsGer |
(DE-627)NLEJ186301448 (DE-599)GBVNLZ186301448 DE-627 ger DE-627 rakwb eng A deletion mutation in glucosephosphate isomerase (GPI denton) 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Yuan, P.M. oth Zaun, M.R. oth Kester, M.V. oth Snider, C.E. oth Johnson, M. oth Gracy, R.W. oth in Clinica Chimica Acta Amsterdam : Elsevier 92(1979), 3, Seite 481-489 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:92 year:1979 number:3 pages:481-489 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 92 1979 3 481-489 |
| allfieldsSound |
(DE-627)NLEJ186301448 (DE-599)GBVNLZ186301448 DE-627 ger DE-627 rakwb eng A deletion mutation in glucosephosphate isomerase (GPI denton) 1979 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 Yuan, P.M. oth Zaun, M.R. oth Kester, M.V. oth Snider, C.E. oth Johnson, M. oth Gracy, R.W. oth in Clinica Chimica Acta Amsterdam : Elsevier 92(1979), 3, Seite 481-489 (DE-627)NLEJ184917921 (DE-600)1499920-1 0009-8981 nnns volume:92 year:1979 number:3 pages:481-489 http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE AR 92 1979 3 481-489 |
| language |
English |
| source |
in Clinica Chimica Acta 92(1979), 3, Seite 481-489 volume:92 year:1979 number:3 pages:481-489 |
| sourceStr |
in Clinica Chimica Acta 92(1979), 3, Seite 481-489 volume:92 year:1979 number:3 pages:481-489 |
| format_phy_str_mv |
Article |
| institution |
findex.gbv.de |
| isfreeaccess_bool |
false |
| container_title |
Clinica Chimica Acta |
| authorswithroles_txt_mv |
Yuan, P.M. @@oth@@ Zaun, M.R. @@oth@@ Kester, M.V. @@oth@@ Snider, C.E. @@oth@@ Johnson, M. @@oth@@ Gracy, R.W. @@oth@@ |
| publishDateDaySort_date |
1979-01-01T00:00:00Z |
| hierarchy_top_id |
NLEJ184917921 |
| id |
NLEJ186301448 |
| 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">NLEJ186301448</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707042332.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1979 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186301448</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186301448</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="2"><subfield code="a">A deletion mutation in glucosephosphate isomerase (GPI denton)</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1979</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">A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yuan, P.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zaun, M.R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kester, M.V.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Snider, C.E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Johnson, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gracy, R.W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Clinica Chimica Acta</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">92(1979), 3, Seite 481-489</subfield><subfield code="w">(DE-627)NLEJ184917921</subfield><subfield code="w">(DE-600)1499920-1</subfield><subfield code="x">0009-8981</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:92</subfield><subfield code="g">year:1979</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:481-489</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</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">92</subfield><subfield code="j">1979</subfield><subfield code="e">3</subfield><subfield code="h">481-489</subfield></datafield></record></collection>
|
| series2 |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| ppnlink_with_tag_str_mv |
@@773@@(DE-627)NLEJ184917921 |
| format |
electronic Article |
| delete_txt_mv |
keep |
| collection |
NL |
| remote_str |
true |
| illustrated |
Not Illustrated |
| issn |
0009-8981 |
| topic_title |
A deletion mutation in glucosephosphate isomerase (GPI denton) |
| format_facet |
Elektronische Aufsätze Aufsätze Elektronische Ressource |
| format_main_str_mv |
Text Zeitschrift/Artikel |
| carriertype_str_mv |
zu |
| author2_variant |
p y py m z mz m k mk c s cs m j mj r g rg |
| hierarchy_parent_title |
Clinica Chimica Acta |
| hierarchy_parent_id |
NLEJ184917921 |
| hierarchy_top_title |
Clinica Chimica Acta |
| isfreeaccess_txt |
false |
| familylinks_str_mv |
(DE-627)NLEJ184917921 (DE-600)1499920-1 |
| title |
A deletion mutation in glucosephosphate isomerase (GPI denton) |
| spellingShingle |
A deletion mutation in glucosephosphate isomerase (GPI denton) |
| ctrlnum |
(DE-627)NLEJ186301448 (DE-599)GBVNLZ186301448 |
| title_full |
A deletion mutation in glucosephosphate isomerase (GPI denton) |
| journal |
Clinica Chimica Acta |
| journalStr |
Clinica Chimica Acta |
| lang_code |
eng |
| isOA_bool |
false |
| recordtype |
marc |
| publishDateSort |
1979 |
| contenttype_str_mv |
zzz |
| container_start_page |
481 |
| container_volume |
92 |
| format_se |
Elektronische Aufsätze |
| title_sort |
deletion mutation in glucosephosphate isomerase (gpi denton) |
| title_auth |
A deletion mutation in glucosephosphate isomerase (GPI denton) |
| abstract |
A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. |
| abstractGer |
A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. |
| abstract_unstemmed |
A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation. |
| collection_details |
GBV_USEFLAG_H ZDB-1-SDJ GBV_NL_ARTICLE |
| container_issue |
3 |
| title_short |
A deletion mutation in glucosephosphate isomerase (GPI denton) |
| url |
http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6 |
| remote_bool |
true |
| author2 |
Yuan, P.M. Zaun, M.R. Kester, M.V. Snider, C.E. Johnson, M. Gracy, R.W. |
| author2Str |
Yuan, P.M. Zaun, M.R. Kester, M.V. Snider, C.E. Johnson, M. Gracy, R.W. |
| ppnlink |
NLEJ184917921 |
| mediatype_str_mv |
z |
| isOA_txt |
false |
| hochschulschrift_bool |
false |
| author2_role |
oth oth oth oth oth oth |
| up_date |
2024-07-06T06:32:26.234Z |
| _version_ |
1803810291041959936 |
| 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">NLEJ186301448</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210707042332.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070506s1979 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ186301448</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-599)GBVNLZ186301448</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="2"><subfield code="a">A deletion mutation in glucosephosphate isomerase (GPI denton)</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1979</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">A new genetic variant form of glucosephosphate isomerase has been found in a family heterozygous for the mutant allele. The mutant enzyme, unlike other phenotypic variants, does not appear to be the result of a single amino acid replacement. The allozyme exhibits an isoelectric point of 5.7 and is thus much more acidic than the normal enzyme (pI = 9.3). The allozyme has been isolated from placenta and separated from the normal homodimer and heterodimer by isoelectric focusing. The enzyme exhibits normal k"m and K"i values for the substrates and competitive inhibitors. The allozyme exhibits a normal pH optimum and thermal stability. However, the molecular specific activity of the variant enzyme as quantitated by radioimmunoassay is significantly lower than normal. Analytical gel filtration revealed that the molecular weight of the enzyme is significantly lower than the normal enzyme. These data thus suggest that the phenotype is unlike any previously reported and is due to a deletion mutation.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Elsevier Journal Backfiles on ScienceDirect 1907 - 2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Yuan, P.M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zaun, M.R.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Kester, M.V.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Snider, C.E.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Johnson, M.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gracy, R.W.</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Clinica Chimica Acta</subfield><subfield code="d">Amsterdam : Elsevier</subfield><subfield code="g">92(1979), 3, Seite 481-489</subfield><subfield code="w">(DE-627)NLEJ184917921</subfield><subfield code="w">(DE-600)1499920-1</subfield><subfield code="x">0009-8981</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:92</subfield><subfield code="g">year:1979</subfield><subfield code="g">number:3</subfield><subfield code="g">pages:481-489</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://linkinghub.elsevier.com/retrieve/pii/0009-8981(79)90231-6</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_H</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SDJ</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">92</subfield><subfield code="j">1979</subfield><subfield code="e">3</subfield><subfield code="h">481-489</subfield></datafield></record></collection>
|
| score |
7.4004774 |