Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain
Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependen...
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| Autor*in: |
Nijjar, M. S. [verfasserIn] |
|---|
| Format: |
E-Artikel |
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| Erschienen: |
Oxford, UK: Blackwell Publishing Ltd ; 1980 |
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| Umfang: |
Online-Ressource |
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2006 ; Blackwell Publishing Journal Backfiles 1879-2005 |
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In: Journal of neurochemistry - Oxford : Wiley-Blackwell, 1956, 34(1980), 5, Seite 0 |
| Übergeordnetes Werk: |
volume:34 ; year:1980 ; number:5 ; pages:0 |
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| DOI / URN: |
10.1111/j.1471-4159.1980.tb09975.x |
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| 520 | |a Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. | ||
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10.1111/j.1471-4159.1980.tb09975.x doi (DE-627)NLEJ240327047 DE-627 ger DE-627 rakwb Nijjar, M. S. verfasserin aut Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Brain development In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 34(1980), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:34 year:1980 number:5 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb09975.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 34 1980 5 0 |
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10.1111/j.1471-4159.1980.tb09975.x doi (DE-627)NLEJ240327047 DE-627 ger DE-627 rakwb Nijjar, M. S. verfasserin aut Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Brain development In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 34(1980), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:34 year:1980 number:5 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb09975.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 34 1980 5 0 |
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10.1111/j.1471-4159.1980.tb09975.x doi (DE-627)NLEJ240327047 DE-627 ger DE-627 rakwb Nijjar, M. S. verfasserin aut Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Brain development In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 34(1980), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:34 year:1980 number:5 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb09975.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 34 1980 5 0 |
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10.1111/j.1471-4159.1980.tb09975.x doi (DE-627)NLEJ240327047 DE-627 ger DE-627 rakwb Nijjar, M. S. verfasserin aut Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Brain development In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 34(1980), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:34 year:1980 number:5 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb09975.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 34 1980 5 0 |
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10.1111/j.1471-4159.1980.tb09975.x doi (DE-627)NLEJ240327047 DE-627 ger DE-627 rakwb Nijjar, M. S. verfasserin aut Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain Oxford, UK Blackwell Publishing Ltd 1980 Online-Ressource nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. 2006 Blackwell Publishing Journal Backfiles 1879-2005 |2006|||||||||| Brain development In Journal of neurochemistry Oxford : Wiley-Blackwell, 1956 34(1980), 5, Seite 0 Online-Ressource (DE-627)NLEJ243927584 (DE-600)2020528-4 1471-4159 nnns volume:34 year:1980 number:5 pages:0 http://dx.doi.org/10.1111/j.1471-4159.1980.tb09975.x text/html Verlag Deutschlandweit zugänglich Volltext GBV_USEFLAG_U ZDB-1-DJB GBV_NL_ARTICLE AR 34 1980 5 0 |
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Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain |
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Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. |
| abstractGer |
Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. |
| abstract_unstemmed |
Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. It is concluded that rat brain supernatant contains some factor in addition to CDR which activates particulate adenylate cyclase. |
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S.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Nature of the Cytoplasmic Factor(s) Modulating Adenylate Cyclase in the Developing Rat Brain</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="a">Oxford, UK</subfield><subfield code="b">Blackwell Publishing Ltd</subfield><subfield code="c">1980</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">Online-Ressource</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">Abstract: Adenylate cyclase activity in the particulate fraction from rat brain was markedly enhanced by the cytoplasmic fraction, which itself contained negligible enzyme activity, indicating the presence of some stimulatory factor(s) in the supernatant. Activation of adenylate cyclase was dependent on the supernatant concentration up to 1 mgiml, but higher concentration of the supernatant did not produce further activation of the enzyme. The supernatant retained its stimulatory activity after boiling for 5 min, extensive dialysis, and phospholipase A and DNAase treatments, but was completely inactivated by digestion with trypsin. Ability of the supernatant to activate adenylate cyclase was low during fetal life, increased severalfold neonatally, and declined somewhat thereafter to an adult level. Adenylate cyclase in the particulate fraction from 2-day-old rat brain was also activated by GTP, calcium-dependent regulator (CDR) of cyclic AMP phosphodiesterase in the presence of 100 pM-Ca1, and by NaF. The supernatant produced additive activation of the enzyme with NaF but not with GTP or CDR, suggesting a common site of action of the supernatant factor(s) and the latter two agents. DEAE-cellulose chromatography of the boiled supernatant resolved the heat-stable proteins into several peaks. Adenylate cyclase activator eluted in two distinct peaks, one of which also contained CDR activity. 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