The enzymic synthesis and degradation of starch. Part XIX. The action of R-enzyme on glycogen

Stanley Peat, William J. Whelan, P. N. Hobson, Gwen J. Thomas

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

It is shown that R-enzyme, which debranches amylopectin, does not exert a similar hydrolytic action on the glycogen from oysters or from rabbit liver. Evidence is adduced to support the view that this lack of action is due to the higher degree of branching of the glycogen and consequently to the greater compactness of the molecule which makes the majority of the branch links inaccessible to the enzyme. It is worthy of note that the action of R-enzyme provides a simple practical method of distinguishing amylopectins from glycogens.

Original languageEnglish
Pages (from-to)4440-4445
Number of pages6
JournalJournal of the Chemical Society (Resumed)
DOIs
StatePublished - Dec 1 1954
Externally publishedYes

Fingerprint

Glycogen
Starch
Amylopectin
Degradation
Enzymes
Ostreidae
Liver
Rabbits
Molecules

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

The enzymic synthesis and degradation of starch. Part XIX. The action of R-enzyme on glycogen. / Peat, Stanley; Whelan, William J.; Hobson, P. N.; Thomas, Gwen J.

In: Journal of the Chemical Society (Resumed), 01.12.1954, p. 4440-4445.

Research output: Contribution to journalArticle

@article{34d1a1eeca66429781e757208c45de00,
title = "The enzymic synthesis and degradation of starch. Part XIX. The action of R-enzyme on glycogen",
abstract = "It is shown that R-enzyme, which debranches amylopectin, does not exert a similar hydrolytic action on the glycogen from oysters or from rabbit liver. Evidence is adduced to support the view that this lack of action is due to the higher degree of branching of the glycogen and consequently to the greater compactness of the molecule which makes the majority of the branch links inaccessible to the enzyme. It is worthy of note that the action of R-enzyme provides a simple practical method of distinguishing amylopectins from glycogens.",
author = "Stanley Peat and Whelan, {William J.} and Hobson, {P. N.} and Thomas, {Gwen J.}",
year = "1954",
month = "12",
day = "1",
doi = "10.1039/JR9540004440",
language = "English",
pages = "4440--4445",
journal = "Journal of the Chemical Society",
issn = "0577-6171",
publisher = "Chemical Society",

}

TY - JOUR

T1 - The enzymic synthesis and degradation of starch. Part XIX. The action of R-enzyme on glycogen

AU - Peat, Stanley

AU - Whelan, William J.

AU - Hobson, P. N.

AU - Thomas, Gwen J.

PY - 1954/12/1

Y1 - 1954/12/1

N2 - It is shown that R-enzyme, which debranches amylopectin, does not exert a similar hydrolytic action on the glycogen from oysters or from rabbit liver. Evidence is adduced to support the view that this lack of action is due to the higher degree of branching of the glycogen and consequently to the greater compactness of the molecule which makes the majority of the branch links inaccessible to the enzyme. It is worthy of note that the action of R-enzyme provides a simple practical method of distinguishing amylopectins from glycogens.

AB - It is shown that R-enzyme, which debranches amylopectin, does not exert a similar hydrolytic action on the glycogen from oysters or from rabbit liver. Evidence is adduced to support the view that this lack of action is due to the higher degree of branching of the glycogen and consequently to the greater compactness of the molecule which makes the majority of the branch links inaccessible to the enzyme. It is worthy of note that the action of R-enzyme provides a simple practical method of distinguishing amylopectins from glycogens.

UR - http://www.scopus.com/inward/record.url?scp=31344480595&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=31344480595&partnerID=8YFLogxK

U2 - 10.1039/JR9540004440

DO - 10.1039/JR9540004440

M3 - Article

AN - SCOPUS:31344480595

SP - 4440

EP - 4445

JO - Journal of the Chemical Society

JF - Journal of the Chemical Society

SN - 0577-6171

ER -