Enzymic conversion of phosphorylase a to phosphorylase b

Keller, Patricia J.; Cori, Gerty T.

doi:10.1016/0006-3002(53)90142-5

Cited by 130 publications

(37 citation statements)

References 5 publications

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“…The position of haemoglobin was determined from its A411. Sedimentation coefficients of 8.2 S for phosphorylase (Keller & Cori, 1953), 4.6S for haemoglobin (Schachman & Edelstein, 1966) and 11.2S for catalase (Sumner & Gralen, 1938) were used to calculate unknown sedimentation coefficients. In each gradient, the plot of migration of standard proteins versus sedimentation coefficient was linear.…”

Section: Deae-cellulose Chromatographymentioning

confidence: 99%

Protein kinase activities in rat pancreatic islets of Langerhans

Sugden¹,

Ashcroft²,

Sugden³

1979

Biochemical Journal

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[218][219][220][221][222][223][224][225], and the fourth species was a cyclic AMPindependent protein kinase. 5. Determination of physical and kinetic properties of the protein kinases showed that the properties of the cyclic AMP-dependent activities were similar to those described in other tissues and were clearly distinct from those of the cyclic AMP-independent protein kinase. 6. The cyclic AMP-independent protein kinase had an S20.w of 5.2S, phosphorylated a serine residue(s) in casein and was not inhibited by the cyclic AMP-dependent protein kinase inhibitor. 7. These studies demonstrate the existence in rat islets of Langerhans of multiple forms of cyclic AMP-dependent protein kinase and also the presence of a cyclic AMP-independent protein kinase distinct from the free catalytic subunit of cyclic AMP-dependent protein kinase. The presence of the cyclic AMPindependent protein kinase may account for the observed characteristics of 32p incorporation into endogenous protein in homogenates of rat islets.

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Section: Deae-cellulose Chromatographymentioning

confidence: 99%

Protein kinase activities in rat pancreatic islets of Langerhans

Sugden¹,

Ashcroft²,

Sugden³

1979

Biochemical Journal

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show abstract

“…Phosphorylase b was shown to have a m.w. of 242,000, half that of phosphorylase a (495,000) (25)(26)(27). These investigators demonstrated that both phosphorylase b and a can further dissociate into subunits of m.w.…”

Section: Molecular Weightmentioning

confidence: 99%

Molecular Properties and Transformations of Glycogen Phosphorylase in Animal Tissues

Krebs

Fischer

1962

Advances in Enzymology - And Related Areas of Molecular Biology

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“…In B. subtilis, also, the formation of amylase involves the transformation of a precursor protein (248). Phosphorylase a results from the phosphorylation of four serine residues of phosphorylase b followed by dimerization (75,133,141). The activation of trypsinogen and chymotrypsogen results from a spontaneous change in the tertiary structure which occurs when a peptide bond is broken (166).…”

Section: Release Of the Polypeptide From The Template Andmentioning

confidence: 99%

Aspects of the Biosynthesis of Enzymes

Chantrenne¹

1962

Advances in Enzymology - And Related Areas of Molecular Biology

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Enzymic conversion of phosphorylase a to phosphorylase b

Cited by 130 publications

References 5 publications

Protein kinase activities in rat pancreatic islets of Langerhans

Protein kinase activities in rat pancreatic islets of Langerhans

Molecular Properties and Transformations of Glycogen Phosphorylase in Animal Tissues

Aspects of the Biosynthesis of Enzymes

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