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Action of two alkaline proteases and a trypsin inhibitor from white croaker skeletal muscle ( Micropogon opercularis ) in the degradation of myofibrillar proteins
Author(s) -
Folco E.J.,
Busconi L.,
Marione C.,
Trucco R.E.,
Sánchez J.J.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)80944-8
Subject(s) - proteases , myofibril , myosin , biochemistry , protease , protease inhibitor (pharmacology) , trypsin , chemistry , skeletal muscle , enzyme , biology , anatomy , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , immunology
The action of two alkaline proteases from white skeletal muscle on myofibrillar proteins is shown. Purified myosin was readily degraded by both proteases, but only protease I was able to degrade myosin heavy chain from actomyosin. The effect of inhibitor on both proteases was also studied. The activity of protease II on azocasein was not affected, while the action of protease I on both azocasein and myosin was inhibited. The implication of proteases and inhibitor on the turnover of myofibrillar proteins is considered.