Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Research Abstract Details 

Research Abstract Table of Contents

Jump to the:

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Abstract Text:

S Ishiura,H Murofushi,K Suzuki,K Imahori,

A calcium-activated neutral protease was purified 2,700-fold over the crude extract from chicken skeletal muscle. The purified protease migrated as a single band on polyacrylamide gel electrophoresis with or without SDS. Its molecular weight was 80,000 and pH optimum for activity was 7.7. The activity required strictly the presence of calcium (optimum concentration: 1.8 mM) or strontium (optimum concentration: 10 mM) ions. The protease was inhibited by leupeptin, which is known to be a strong inhibitor of papain, cathepsin B, trypsin, and plasmin.

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Publishing Authors By Initials

S Ishiura,H Murofushi,K Suzuki,K Imahori,

For similar inorganic chemicals: elements: metals, alkaline earth: strontium research abstracts see: inorganic chemicals: elements: metals, alkaline earth: strontium research

PUBMED ID PMID:

MEDLINE DATE:

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 84

Page Numbers: 225-30

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Jul

YEAR: 1978

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 376600

Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Keywords Mesh Terms:

KEYWORDS: Strontium

MESH TERMS: pharmacology

Chemical & Substance for Abstract: Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization. Information

Substance Name: Peptide Hydrolases

Registry Number: EC 3.4.-

Grant and Affiliation Information for Studies of a calcium-activated neutral protease from chicken skeletal muscle. I. Purification and characterization.

AFFILIATION:

Country: JAPAN

AGENCY:

GRANT:

ACRONYM:

MEDLINETA: J Biochem

REFSOURCE:

DATABASENAME:

ACCESSION NUMBER:

Number Hits: 0

Studies of a calcium-activated neutral protease from chicken skeletal muscle I Purification and characterization 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.