Characterization of muscle low calcium requiring form of calcium activated protease.

• OTSUKA Yuzuru

  College of Education, Tottori University

• FUJITA Hiromi

  College of Education, Tottori University

• INOSAKO Yasue

  College of Education, Tottori University

• KUMOJIMA Yoko

  College of Education, Tottori University

• ICHIMURA Fumiko

  College of Education, Tottori University

• IKEMOTO Etsuko

  College of Education, Tottori University

• KAWABARA Eiko

  Laboratory of Electronmicroscope, College of Agriculture, Tottori University

Abstract

A low calcium requiring form of calcium activated protease (LCAP) and a high calcium requiring form of calcium activated protease (HCAP), purified from porcine skeletal muscle, were studied. LCAP was most active at pH 8.2. The HCAP was rather unstable at high temperature or at alkaline pHs: The antiserum to purified LCAP did not make a precipitin line with HCAP. Those proteases hydrolyzed myofibril proteins to disassemble the structure of myofibrils. The electronmicrogram of the myofibril treated by LCAP resembled that of the muscle obtained from a vitamin E deficient rat. Both LCAP and HCAP hydrolyzed purified α-actinin, liver actin, and some other proteins which are not assigned. The microsome proteins were resistant to protease treatment, and only the 180kd protein was hydrolyzed by LCAP.

Journal

• Agricultural and Biological Chemistry

  Agricultural and Biological Chemistry 52 (1), 31-40, 1988

  Japan Society for Bioscience, Biotechnology, and Agrochemistry

Keywords

• General Agricultural and Biological Sciences
• General Biochemistry, Genetics and Molecular Biology

Details

• CRID: 1390282681442296960
• NII Article ID: 110006323419
• NII Book ID: AA00515312
• DOI: 10.1271/bbb1961.52.31
• ISSN: 18811280
• ISSN: 00021369
• Text Lang: en
• Data Source:
  • JaLC
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed