A comparative study of crystallized silky and lemon shark muscle glycogen phosphorylases

Sáid A. Assaf, Adel A Yunis

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

1. 1. Silky and lemon shark muscle glycogen phosphorylases b and a were purified and crystallized under similar conditions. In contrast to other phosphorylases, both enzymes crystallize from ammonium sulphate or buffer. The doubling in molecular weight observed upon phosphorylation to the a form is similar to that of homoiothenns but different from that of other poikilotherms (frog and lobster). 2. 2. The enzymes from these a shark species are more stable than those from muscle of homoiotherms and, like lobster phosphorylase, they require no sulphydryl compounds for maintaining their activity. 3. 3. Lemon and silky shark phosphorylases appear to be immunologically identical and distinct from the phosphorylases of rabbit or human muscle. 4. 4. The fact that phosphorylase from lemon or silky shark can be prepared in homogenous form, crystallized, and stabilized in dilute buffer without need for the activator 5/-AMP, sulphydryl compounds, or a high concentration of salts, makes it unique among the glycogen phosphorylases and particularly useful for research purposes.

Original languageEnglish (US)
Pages (from-to)604-608
Number of pages5
JournalInternational Journal of Biochemistry
Volume2
Issue number11
DOIs
StatePublished - 1971

Fingerprint

Glycogen Phosphorylase
Sharks
Phosphorylases
Muscle
Muscles
Buffers
Phosphorylase b
Phosphorylase a
Phosphorylation
Ammonium Sulfate
Enzymes
Adenosine Monophosphate
Anura
Salts
Molecular Weight
Molecular weight
Rabbits
Research

Keywords

  • Carcharhinus faiciformis
  • comparative studies on glycogen phosphorylase of poikilotherms and homoiotherms
  • crystallization
  • immunological behaviour
  • JVegaprion brevirostris
  • lemon shark
  • molecular weight
  • Silky shark
  • solubility
  • stability
  • sulphydryl groups

ASJC Scopus subject areas

  • Biochemistry

Cite this

A comparative study of crystallized silky and lemon shark muscle glycogen phosphorylases. / Assaf, Sáid A.; Yunis, Adel A.

In: International Journal of Biochemistry, Vol. 2, No. 11, 1971, p. 604-608.

Research output: Contribution to journalArticle

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AB - 1. 1. Silky and lemon shark muscle glycogen phosphorylases b and a were purified and crystallized under similar conditions. In contrast to other phosphorylases, both enzymes crystallize from ammonium sulphate or buffer. The doubling in molecular weight observed upon phosphorylation to the a form is similar to that of homoiothenns but different from that of other poikilotherms (frog and lobster). 2. 2. The enzymes from these a shark species are more stable than those from muscle of homoiotherms and, like lobster phosphorylase, they require no sulphydryl compounds for maintaining their activity. 3. 3. Lemon and silky shark phosphorylases appear to be immunologically identical and distinct from the phosphorylases of rabbit or human muscle. 4. 4. The fact that phosphorylase from lemon or silky shark can be prepared in homogenous form, crystallized, and stabilized in dilute buffer without need for the activator 5/-AMP, sulphydryl compounds, or a high concentration of salts, makes it unique among the glycogen phosphorylases and particularly useful for research purposes.

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