Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism
Initial rate and affinity studies on mantle Mytilus phosphorylase a were carried out in order to find possible differences in its kinetic properties with respect to phosphorylase b. Phosphorylase a was not stimulated for any AMP concentrations. Michaelis constants ( K m) are 0.05 mg/ml glycogen, 1.1...
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| Veröffentlicht in: | The international journal of biochemistry & cell biology 1995-09, Vol.27 (9), p.917-922 |
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| container_title | The international journal of biochemistry & cell biology |
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| creator | Serrano, Fuencisla San Juan González, Margarita Fernández López, JoséLuis Sánchez Martín, L.Oscar Garcia |
| description | Initial rate and affinity studies on mantle
Mytilus phosphorylase a were carried out in order to find possible differences in its kinetic properties with respect to phosphorylase b. Phosphorylase a was not stimulated for any AMP concentrations. Michaelis constants (
K
m) are 0.05 mg/ml glycogen, 1.15 mM inorganic phosphate and 1.50 mM glucose-1-phosphate. The
K
ms for the substrates, in the direction of glycogen breakdown, are enhanced by non-saturating concentrations of cosubstrate, without reducing the apparent maximum velocity. First order and hyperbolic kinetics and values of the allosteric constant smaller than 2 were observed. These results suggest a catalytic mechanism different to that shown for mantle
Mytilus phosphorylase b. |
| doi_str_mv | 10.1016/1357-2725(95)00059-X |
| format | Article |
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Mytilus phosphorylase a were carried out in order to find possible differences in its kinetic properties with respect to phosphorylase b. Phosphorylase a was not stimulated for any AMP concentrations. Michaelis constants (
K
m) are 0.05 mg/ml glycogen, 1.15 mM inorganic phosphate and 1.50 mM glucose-1-phosphate. The
K
ms for the substrates, in the direction of glycogen breakdown, are enhanced by non-saturating concentrations of cosubstrate, without reducing the apparent maximum velocity. First order and hyperbolic kinetics and values of the allosteric constant smaller than 2 were observed. These results suggest a catalytic mechanism different to that shown for mantle
Mytilus phosphorylase b.</description><identifier>ISSN: 1357-2725</identifier><identifier>EISSN: 1878-5875</identifier><identifier>DOI: 10.1016/1357-2725(95)00059-X</identifier><identifier>PMID: 7584627</identifier><language>eng</language><publisher>Netherlands: Elsevier Ltd</publisher><subject>Adenosine Monophosphate - pharmacology ; Animals ; Bivalvia - enzymology ; Glycogen - metabolism ; Kinetic parameters ; Kinetics ; Mytilus ; Phosphates - metabolism ; Phosphorylase ; Phosphorylase a - metabolism ; Phosphorylase b - metabolism ; Phosphorylases - metabolism ; Phosphorylation ; Substrate Specificity</subject><ispartof>The international journal of biochemistry & cell biology, 1995-09, Vol.27 (9), p.917-922</ispartof><rights>1995</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c306t-c8bafcecb203989afa8207157922e163b3e1279235d2192e2bd1cabd101b6253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/1357-2725(95)00059-X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7584627$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Serrano, Fuencisla San Juan</creatorcontrib><creatorcontrib>González, Margarita Fernández</creatorcontrib><creatorcontrib>López, JoséLuis Sánchez</creatorcontrib><creatorcontrib>Martín, L.Oscar Garcia</creatorcontrib><title>Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism</title><title>The international journal of biochemistry & cell biology</title><addtitle>Int J Biochem Cell Biol</addtitle><description>Initial rate and affinity studies on mantle
Mytilus phosphorylase a were carried out in order to find possible differences in its kinetic properties with respect to phosphorylase b. Phosphorylase a was not stimulated for any AMP concentrations. Michaelis constants (
K
m) are 0.05 mg/ml glycogen, 1.15 mM inorganic phosphate and 1.50 mM glucose-1-phosphate. The
K
ms for the substrates, in the direction of glycogen breakdown, are enhanced by non-saturating concentrations of cosubstrate, without reducing the apparent maximum velocity. First order and hyperbolic kinetics and values of the allosteric constant smaller than 2 were observed. These results suggest a catalytic mechanism different to that shown for mantle
Mytilus phosphorylase b.</description><subject>Adenosine Monophosphate - pharmacology</subject><subject>Animals</subject><subject>Bivalvia - enzymology</subject><subject>Glycogen - metabolism</subject><subject>Kinetic parameters</subject><subject>Kinetics</subject><subject>Mytilus</subject><subject>Phosphates - metabolism</subject><subject>Phosphorylase</subject><subject>Phosphorylase a - metabolism</subject><subject>Phosphorylase b - metabolism</subject><subject>Phosphorylases - metabolism</subject><subject>Phosphorylation</subject><subject>Substrate Specificity</subject><issn>1357-2725</issn><issn>1878-5875</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kctu1TAQhi1EVdrCG4DkFYJFii_HcbJBqiooSK3YdNGd5TiTU4MTHzxOpTwDL12n54BYdeHrfPOP_Q8hbzk754zXn7hUuhJaqA-t-sgYU21194Kc8EY3lWq0eln2f5FX5BTxZ4G4EvKYHGvVbGqhT8ifm9j7wTubfZxoHOgvP0H2ju5ssiNkSLjebsPi4hYmuruPWEZagkWgQ4ojHe2UA9DsEWdY4Zsl-zAj3doQ4i7FBz85b4NH2i3U_i_xVHQEd28nj-NrcjTYgPDmsJ6R269fbi-_Vdc_rr5fXlxXTrI6V67p7ODAdYLJtmntYBvBNFe6FQJ4LTsJXJSDVL3grQDR9dzZMjHe1ULJM_J-L1ue9nsGzGb06CAEO0Gc0WitpGJqU8DNHnQpIiYYzC750abFcGbWFpjVX7P6a1plnlpg7krau4P-3I3Q_0s6eF7in_dxKH988JAMOg-Tg94ncNn00T9f4BHG5Jn6</recordid><startdate>19950901</startdate><enddate>19950901</enddate><creator>Serrano, Fuencisla San Juan</creator><creator>González, Margarita Fernández</creator><creator>López, JoséLuis Sánchez</creator><creator>Martín, L.Oscar Garcia</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>19950901</creationdate><title>Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism</title><author>Serrano, Fuencisla San Juan ; González, Margarita Fernández ; López, JoséLuis Sánchez ; Martín, L.Oscar Garcia</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c306t-c8bafcecb203989afa8207157922e163b3e1279235d2192e2bd1cabd101b6253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Adenosine Monophosphate - pharmacology</topic><topic>Animals</topic><topic>Bivalvia - enzymology</topic><topic>Glycogen - metabolism</topic><topic>Kinetic parameters</topic><topic>Kinetics</topic><topic>Mytilus</topic><topic>Phosphates - metabolism</topic><topic>Phosphorylase</topic><topic>Phosphorylase a - metabolism</topic><topic>Phosphorylase b - metabolism</topic><topic>Phosphorylases - metabolism</topic><topic>Phosphorylation</topic><topic>Substrate Specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serrano, Fuencisla San Juan</creatorcontrib><creatorcontrib>González, Margarita Fernández</creatorcontrib><creatorcontrib>López, JoséLuis Sánchez</creatorcontrib><creatorcontrib>Martín, L.Oscar Garcia</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The international journal of biochemistry & cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Serrano, Fuencisla San Juan</au><au>González, Margarita Fernández</au><au>López, JoséLuis Sánchez</au><au>Martín, L.Oscar Garcia</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism</atitle><jtitle>The international journal of biochemistry & cell biology</jtitle><addtitle>Int J Biochem Cell Biol</addtitle><date>1995-09-01</date><risdate>1995</risdate><volume>27</volume><issue>9</issue><spage>917</spage><epage>922</epage><pages>917-922</pages><issn>1357-2725</issn><eissn>1878-5875</eissn><abstract>Initial rate and affinity studies on mantle
Mytilus phosphorylase a were carried out in order to find possible differences in its kinetic properties with respect to phosphorylase b. Phosphorylase a was not stimulated for any AMP concentrations. Michaelis constants (
K
m) are 0.05 mg/ml glycogen, 1.15 mM inorganic phosphate and 1.50 mM glucose-1-phosphate. The
K
ms for the substrates, in the direction of glycogen breakdown, are enhanced by non-saturating concentrations of cosubstrate, without reducing the apparent maximum velocity. First order and hyperbolic kinetics and values of the allosteric constant smaller than 2 were observed. These results suggest a catalytic mechanism different to that shown for mantle
Mytilus phosphorylase b.</abstract><cop>Netherlands</cop><pub>Elsevier Ltd</pub><pmid>7584627</pmid><doi>10.1016/1357-2725(95)00059-X</doi><tpages>6</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1357-2725 |
| ispartof | The international journal of biochemistry & cell biology, 1995-09, Vol.27 (9), p.917-922 |
| issn | 1357-2725 1878-5875 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Adenosine Monophosphate - pharmacology Animals Bivalvia - enzymology Glycogen - metabolism Kinetic parameters Kinetics Mytilus Phosphates - metabolism Phosphorylase Phosphorylase a - metabolism Phosphorylase b - metabolism Phosphorylases - metabolism Phosphorylation Substrate Specificity |
| title | Modification of kinetic parameters of glycogen phosphorylase from mantle tissue of Mytilus galloprovincialis by a phosphorylation mechanism |
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