Effect of a Serine Protease on Isolated Myofibrils1
- 1 February 1979
- journal article
- research article
- Published by Oxford University Press (OUP) in The Journal of Biochemistry
- Vol. 85 (2) , 481-483
- https://doi.org/10.1093/oxfordjournals.jbchem.a132354
Abstract
Morphological changes occurred in myofibrils prepared from the glycerinated psoas muscle of rabbit during incubation with a serine protease crystallized from rat skeletal muscle. Two notable phenomena were observed: (1) loss of the Z band in the early stage of incubation and (2) complete disappearance of the A band after swelling of the myofibrils. The results indicate that the serine protease has an action on myofibrils different from that of Ca2+ dependent neutral protease.This publication has 7 references indexed in Scilit:
- Studies of a Calcium-Activated Neutral Protease from Chicken Skeletal MuscleThe Journal of Biochemistry, 1978
- Purification and characterization of a myosin-cleaving protease from rat heart myofibrilsBiochimica et Biophysica Acta (BBA) - Enzymology, 1978
- Susceptibilities of Various Myofibrillar Proteins to Muscle Serine Protease1The Journal of Biochemistry, 1978
- Crystallization and amino acid composition of a serine protease from rat skeletal muscleBiochemical and Biophysical Research Communications, 1978
- Preparative Study on the Isolation of Single Sarcomeres from Rabbit Skeletal MuscleThe Journal of Biochemistry, 1978
- A calcium(2+) ion-activated protease possibly involved in myofibrillar protein turnover. Partial characterization of the purified enzymeBiochemistry, 1976
- A Ca2+ion-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscleBiochemistry, 1976