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Biological Chemistry Volume 382 Issue 5

Subject Areas: Biochemistry; ;
Publisher: Walter de Gruyter - de Gruyter
ISSN: 1431-6730
SJR: 123

LitStream

Journal Article

Autolysis of µ- and m-Calpain from Bovine Skeletal Muscle

Cottin, P.; Thompson, V.F.; Sathe, S.K.; Szpacenko, A.; Goll, D.E.

2001 Biological Chemistry

doi:10.1515/BC.2001.092 pmid:11517929

Abstract The rate of autolysis of and mcalpain from bovine skeletal muscle was measured by using densitometry of SDS polyacrylamide gels and determining the rate of disappearance of the 28 and 80 kDa subunits of the native, unautolyzed calpain molecules. Rate of autolysis of both the 28 and 80...
LitStream

Journal Article

Structural Basis for Possible Calcium-Induced Activation Mechanisms of Calpains

Reverter, D.; Strobl, S.; Fernandez-Catalan, C.; Sorimachi, H.; Suzuki, K.; Bode, W.

2001 Biological Chemistry

doi:10.1515/BC.2001.091 pmid:11517928

Abstract The calpains form a growing family of structurally related intracellular multidomainal cysteine proteinases, which exhibit a catalytic domain distantly related to papain. In contrast to papain, however, their activity in most cases depends on calcium. The calpains are believed to play...
LitStream

Journal Article

Properties of a Milk Clotting Protease Isolated from Fruits of Bromelia balansae Mez

Pardo, M.F.; López, L.M.I.; Caffini, N.O.; Natalucci, C.L.

2001 Biological Chemistry

doi:10.1515/BC.2001.107 pmid:11517944

Abstract Unripe fruit extracts of Bromelia balansae Mez Bromeliaceae), whose principal endopeptidase is balansain I (isolated for anion exchange chromatography: pI = 5.45, molecular weight = 23192), exhibit pH profile with a maximum activity around pH 9.0 and are inhibited only by cysteine...
LitStream

Journal Article

Evolutionary Lines of Cysteine Peptidases

Barrett, A.J.; Rawlings, N.D.

2001 Biological Chemistry

doi:10.1515/BC.2001.088 pmid:11517925

Abstract The proteolytic enzymes that depend upon a cysteine residue for activity have come from at least seven different evolutionary origins, each of which has produced a group of cysteine peptidases with distinctive structures and properties. We show here that the characteristic molecular...
LitStream

Journal Article

Towards Specific Functions of Lysosomal Cysteine Peptidases: Phenotypes of Mice Deficient for Cathepsin B or Cathepsin L

Reinheckel, T.; Deussing, J.; Roth, W.; Peters, C.

2001 Biological Chemistry

doi:10.1515/BC.2001.089 pmid:11517926

Abstract The lysosomal cysteine peptidases cathepsin B and cathepsin L are abundant and ubiquitously expressed members of the papain family, and both enzymes contribute to the terminal degradation of proteins in the lysosome. However, there is accumulating evidence for specific functions of...

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