Characterization of calpains and calpastatins from hamster skeletal muscle.
1. Hamster skeletal muscle contains a wide-specificity calpain which was found to be a calpain II type and which is composed of a single Mr 80,000 polypeptide. 2. The muscle also contains a calpain I type enzyme which is specific for desmin degradation, and this enzyme consists of a single subunit of Mr 67,000. 3. Three calpastatins were detected in the tissue, one of which inhibited both calpains, whereas the other two appeared to be specific for the desmin-specific calpain. These calpastatins possessed the same inhibition properties when assayed with chicken gizzard calpains.
Johnson
P
P
Department of Chemistry, Ohio University, Athens 45701.
Guindon-Hammer
J L
JL
D000818:Animals; D002135:Calcium-Binding Proteins / Q000302:isolation & purification*; D002154:Calpain / Q000037:antagonists & inhibitors / Q000302:isolation & purification* / Q000378:metabolism; D002850:Chromatography, Gel / Q000379:methods; D002852:Chromatography, Ion Exchange / Q000379:methods; D006224:Cricetinae; D007525:Isoelectric Focusing / Q000379:methods; D008297:Male; D008647:Mesocricetus; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology*; D011480:Protease Inhibitors / Q000302:isolation & purification*
D002135:Calcium-Binding Proteins; D011480:Protease Inhibitors; C033668:calpastatin; D002154:Calpain