Výsledky vyhledávání - "P L, Vul'fson"

[Association of rabbit skeletal muscle phosphorylase kinase with sarcoplasmic reticulum membranes]

Autor: M A, Zemskova, S A, Shur, L K, Skolysheva, P L, Vul'fson

Publikováno v: Biokhimiia (Moscow, Russia). 60(11)

The binding of phosphorylase kinase to sarcoplasmic reticulum has been studied using gel chromatography. The presence of Ca2+, Mg2+ and glycogen was found to be necessary for the maximal binding. The phosphorylase kinase adsorbed on sarcoplasmic reti

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::13e46316a84aa1f20a924034079276f7
https://pubmed.ncbi.nlm.nih.gov/8590760

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[Formation of a complex between glycogen phosphorylase and creatine kinase in rabbit skeletal muscles]

Autor: A Kh, Khakimova, L K, Skolysheva, S A, Shur, P L, Vul'fson

Publikováno v: Doklady Akademii nauk. 328(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::deb663c27f1565b47d340d774c459b36
https://pubmed.ncbi.nlm.nih.gov/8481686

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[Isolation and properties of three forms of phosphorylase and phosphorylase kinase from human skeletal muscle]

Autor: L K, Skolysheva, S A, Shur, P L, Vul'fson

Publikováno v: Biokhimiia (Moscow, Russia). 57(1)

Three forms of phosphorylase (I, II and III), two of which (I and II) were active in the presence of AMP and one (III) was active without AMP, were isolated from human skeletal muscles. The pI values for phosphorylases b(I) and b(II) were found to be

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::2881721eb2e47c61ccf28c51ca811fbd
https://pubmed.ncbi.nlm.nih.gov/1391203

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[Interaction of phosphorylase kinase with thin filament proteins of rabbit skeletal muscles]

Autor: M A, Zemskova, S A, Shur, L K, Skolysheva, P L, Vul'fson

Publikováno v: Biokhimiia (Moscow, Russia). 56(1)

The binding of phosphorylase kinase to thin filaments and their effects on the enzyme activity as well as the contribution of the enzyme to contractile protein phosphorylation have been studied. The data obtained suggest that the kinase binding to th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c567bf59d8f1a38fa7bb220e746aeeb8
https://pubmed.ncbi.nlm.nih.gov/1907502

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[The role of histidine residues in the regulation of phosphorylase b activity from rabbit skeletal muscles depending on pH]

Autor: L K, Skolysheva, P L, Vul'fson, S A, Shur, S E, Severin

Publikováno v: Doklady Akademii nauk SSSR. 307(1)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::8abbf3c48a9dc74d017eb298f77a23c7
https://pubmed.ncbi.nlm.nih.gov/2509179

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[Glycogen phosphorylase of skeletal muscles]

Autor: P L, Vul'fson

Publikováno v: Biokhimiia (Moscow, Russia). 51(12)

A review is given on the affinity modification of pyridoxal phosphate and AMP-binding sites as well as on the chemical modification of essential amino acid residues of phosphorylase (histidine residue of the substrate-binding site and cysteine residu

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::9fbc5dc41e35b72c9ce4811d9e558695
https://pubmed.ncbi.nlm.nih.gov/3542060

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[Effect of pH on conformation and kinetic properties of phosphorylase from bovine skeletal muscles]

Autor: L K, Skolysheva, S A, Shur, P L, Vul'fson

Publikováno v: Biokhimiia (Moscow, Russia). 53(9)

Interaction of phosphorylase with 8-anilino-1-naphthalene-sulfonate (ANS) results in the formation of an ANS-protein complex. The microenvironment of the protein-bound dye changes depending on pH. Using fluorimetric titration, the dissociation consta

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::6c8b193c2c9a23f4d8810e61e1156c65
https://pubmed.ncbi.nlm.nih.gov/3203112

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[The role of calmodulin (delta-subunit) in the activation of phosphorylase kinase from rabbit skeletal muscles]

Autor: A N, Pegova, P L, Vul'fson

Publikováno v: Biokhimiia (Moscow, Russia). 51(4)

A comparative study on the structure of nonactivated and activated forms of phosphorylase kinase was carried out. The enzyme was activated by incubation in alkaline medium (pH 8.5), by phosphorylation with cAMP-dependent protein kinase and by limited

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::a280ebd4df4fe70d66400c33f8ff3339
https://pubmed.ncbi.nlm.nih.gov/3011126

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[Interaction of phosphorylase kinase with ATP analogs]

Autor: N V, Guliaeva, R A, Gus'kova, L A, Baranova, N N, Guliaev, P L, Vul'fson

Publikováno v: Doklady Akademii nauk SSSR. 235(3)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c5e4edc4d2bf95c141ffc0ac7fe2f02c
https://pubmed.ncbi.nlm.nih.gov/902571

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[Modification of phosphorylase b histidine residues by diethylpyrocarbonate]

Autor: L K, Skolysheva, P L, Vul'fson, E S, Severin

Publikováno v: Biokhimiia (Moscow, Russia). 42(2)

Interaction of phosphorylase B with diethylpyrocarbonate was studied. It was found that modification of the histidine residues is accompanied by a change in the adsorption spectrum of phosphorylase B at around 240--245 nm, as well as by inhibition of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0a8595d8448d69f2c2792fb60e0b3879
https://pubmed.ncbi.nlm.nih.gov/856305

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