Limited proteolysis by subtilisin reveals structural differences between phosphorylase a and b

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a and b was studied with subtilisin BPN' imobilised to Sepharose 4B. 2. 2. The activity of phosphorylase b is nearly resistant to subtilisin under the conditions (pH 7.0, 30°C) where phosphorylase a rapidly loses its activity. 3. 3. The pH profile of phosphorylase a and b digestion is different. 4. 4. Proteolytic fragments of mol. wt 70,000 and 30,000 generated from phosphorylase a, while mol. wt 80,000 and 70,000 generated 'from phosphorylase b can be detected by SDS gel electrophoresis. 5. 5. Addition of AMP to phosphorylase b favours a conformation similar to-but not identical withphosphorylase a as recognised by subtilisin action.

Original languageEnglish
Pages (from-to)1089-1092
Number of pages4
JournalInternational Journal of Biochemistry
Volume15
Issue number8
DOIs
Publication statusPublished - 1983

Fingerprint

Phosphorylase b
Phosphorylase a
Proteolysis
Subtilisin
Subtilisins
Adenosine Monophosphate
Electrophoresis
Sepharose
Muscle
Conformations
Digestion
Skeletal Muscle
Gels
Rabbits

ASJC Scopus subject areas

  • Biochemistry

Cite this

Limited proteolysis by subtilisin reveals structural differences between phosphorylase a and b. / Dombrádi, V.; Gergely, P.; Bot, G.

In: International Journal of Biochemistry, Vol. 15, No. 8, 1983, p. 1089-1092.

Research output: Contribution to journalArticle

@article{83b4e73e54554dfd990be44a58e5186d,
title = "Limited proteolysis by subtilisin reveals structural differences between phosphorylase a and b",
abstract = "1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a and b was studied with subtilisin BPN' imobilised to Sepharose 4B. 2. 2. The activity of phosphorylase b is nearly resistant to subtilisin under the conditions (pH 7.0, 30°C) where phosphorylase a rapidly loses its activity. 3. 3. The pH profile of phosphorylase a and b digestion is different. 4. 4. Proteolytic fragments of mol. wt 70,000 and 30,000 generated from phosphorylase a, while mol. wt 80,000 and 70,000 generated 'from phosphorylase b can be detected by SDS gel electrophoresis. 5. 5. Addition of AMP to phosphorylase b favours a conformation similar to-but not identical withphosphorylase a as recognised by subtilisin action.",
author = "V. Dombr{\'a}di and P. Gergely and G. Bot",
year = "1983",
doi = "10.1016/0020-711X(83)90049-6",
language = "English",
volume = "15",
pages = "1089--1092",
journal = "International Journal of Biochemistry and Cell Biology",
issn = "1357-2725",
publisher = "Elsevier Limited",
number = "8",

}

TY - JOUR

T1 - Limited proteolysis by subtilisin reveals structural differences between phosphorylase a and b

AU - Dombrádi, V.

AU - Gergely, P.

AU - Bot, G.

PY - 1983

Y1 - 1983

N2 - 1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a and b was studied with subtilisin BPN' imobilised to Sepharose 4B. 2. 2. The activity of phosphorylase b is nearly resistant to subtilisin under the conditions (pH 7.0, 30°C) where phosphorylase a rapidly loses its activity. 3. 3. The pH profile of phosphorylase a and b digestion is different. 4. 4. Proteolytic fragments of mol. wt 70,000 and 30,000 generated from phosphorylase a, while mol. wt 80,000 and 70,000 generated 'from phosphorylase b can be detected by SDS gel electrophoresis. 5. 5. Addition of AMP to phosphorylase b favours a conformation similar to-but not identical withphosphorylase a as recognised by subtilisin action.

AB - 1. 1. The limited proteolysis of rabbit skeletal muscle phosphorylase a and b was studied with subtilisin BPN' imobilised to Sepharose 4B. 2. 2. The activity of phosphorylase b is nearly resistant to subtilisin under the conditions (pH 7.0, 30°C) where phosphorylase a rapidly loses its activity. 3. 3. The pH profile of phosphorylase a and b digestion is different. 4. 4. Proteolytic fragments of mol. wt 70,000 and 30,000 generated from phosphorylase a, while mol. wt 80,000 and 70,000 generated 'from phosphorylase b can be detected by SDS gel electrophoresis. 5. 5. Addition of AMP to phosphorylase b favours a conformation similar to-but not identical withphosphorylase a as recognised by subtilisin action.

UR - http://www.scopus.com/inward/record.url?scp=0020653946&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020653946&partnerID=8YFLogxK

U2 - 10.1016/0020-711X(83)90049-6

DO - 10.1016/0020-711X(83)90049-6

M3 - Article

VL - 15

SP - 1089

EP - 1092

JO - International Journal of Biochemistry and Cell Biology

JF - International Journal of Biochemistry and Cell Biology

SN - 1357-2725

IS - 8

ER -