Autolysis of calcium-activated neutral protease of chicken skeletal muscle.

Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Abstract Text:

K Suzuki,S Tsuji,S Ishiura,Y Kimura,S Kubota,K Imahori,

The conditions and process of autolysis of calcium-activated neutral protease (CANP) were examined. Optimal conditions for autolysis were the same as those required for expression of activity of CANP. The autolysis proceeded rapidly by a strictly limited proteolysis. During autolysis the molecular weight of CANP changed from 82 K (native CANP or mCANP) to 79 K and then 60 K. The 79 K and 60 K molecular species were both active at microM order of Ca2+ (muCANP), whereas the native CANP is active at mM order of Ca2+ (mCANP). Various proteases examined did not produce muCANP from mcanp under the conditions tested. Furthermore, muCANP did not yield muCANP from mCANP at lower Ca2+ concentrations where only muCANP was active. Therefore, muCANP is produced from mCANP only by the specific autolysis of mCANP.

Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Publishing Authors By Initials

K Suzuki,S Tsuji,S Ishiura,Y Kimura,S Kubota,K Imahori,

For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

PUBMED ID PMID:

MEDLINE DATE:

Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 90

Page Numbers: 1787-93

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Dec

YEAR: 1981

Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Keywords Mesh Terms:

KEYWORDS: Temperature

MESH TERMS: metabolism

Chemical & Substance for Abstract: Autolysis of calcium-activated neutral protease of chicken skeletal muscle. Information

Substance Name: Calpain

Registry Number: EC 3.4.22.-

Grant and Affiliation Information for Autolysis of calcium-activated neutral protease of chicken skeletal muscle.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Autolysis of calcium-activated neutral protease of chicken skeletal muscle Related Publications

• A change in circular dichroism due to the binding of guanosine-3-phosphate to ribonuclease T1.
• Affinity labeling of adenine nucleotide-related enzymes with reactive adenine nucleotide analogs. I. Affinity labeling of glyceraldehyde 3-phosphate dehydrogenase and myokinase with a reactive AMP analog.
• Affinity labeling of adenine nucleotide-related enzymes with reactive adenine nucleotide analogs. II. Affinity labeling of phosphoglycerate kinase with a reactive AMP analog.
• CD and fluorescence studies of tRNAPhe from baker's yeast.
• Circular dichroism and conformation of natural and synthetic polynucleotides.
• Conformation of cytidine group in the complex of pancreatic ribonuclease A and cytidine-2'-phosphate.
• Dessociation and reconstitution of colicin E3 and immunity substance complex.
• Difference spectral studies on the interactions between ribonuclease T and its substrate analogues.
• Fluorometric investigation of the local conformation of 16S rRNA in the regions of the 3'- and 5'-ends.
• Fructose-1, 6-bisphosphatase of an extreme thermophile.
• Fructose-diphosphate aldolase of Horseshoe crab (Tachypleus tridentatus).
• Glyceraldehyde 3-phosphate dehydrogenase of Bacillus stearothermophilus. Kinetics and physicochemical studies.
• Glyceraldehyde-3-phosphate dehydrogenase of horseshoe crab (Tachypleus tridentatus).
• Hemodynamic and metabolic changes after carotid endarterectomy in patients with high-degree carotid artery stenosis.
• Hybridization of glyceraldehyde-3-phosphate dehydrogenase in borate.
• Isolation and some properties of glyceraldehyde 3-phosphate dehydrogenase from vegetative cells of Bacillus cereus.
• Phosphoglycerate kinase of Bacillus stearothermophilus.
• Physico-chemical characterization of tyrosyl residues in alpha-chymotrypsinogen and pi-chymotrypsin.
• Physiochemical properties of deoxyribonucleic acid from an extreme thermophile.
• Properties of etiohemoglobin and dimethylprotohemoglobin.
• Protein synthesis in a cell-free system from an extreme thermophile. Effects of preincubation in the cold on polyuridylic acid-dependent polyphenylalanine synthesis at high temperature.
• Purification and characterization of tyrosyl-RNA synthetase from baker's yeast.
• Purification and some properties of DNA-dependent RNA polymerase from an extreme thermophile, Thermus thermophilus HB8.
• Structure of phosphoprotein metabolically active in phosphorylation and dephosphorylation reactions.
• Studies on a thermophilic RNA polymerase which is active only on poly d(A-T) and poly dAdT.
• Studies on an alpha-amylase from a thermophilic bacterium. I. Purification and characterization.
• Studies on phosphoglucomutase from an extreme thermophile, Flavobacterium thermophilum HB8. I. Thermostability and other enzymatic properties.
• Study of circular dichroism of proteins and polypeptides in relation to their backbone and side chain conformations.
• The characterization of newly synthesized RNA in step up cultures of yeast cells.
• The difference in the availabilities of initiation points of phage RNA cistrons in their translation.