Literature DB >> 7026543

Connectin, an elastic protein of muscle. Effects of proteolytic enzymes in situ.

K Maruyama, M Kimura, S Kimura, K Ohashi, K Suzuki, N Katunuma.   

Abstract

The effects of various proteolytic enzymes on the high molecular weight protein (connectin) present in a direct sodium dodecyl sulfate extract of myofibrils from chicken breast muscle were studied in detail. To keep the high molecular weight proteins intact, myofibrils had to be prepared in the presence of EGTA. Trypsin, chymotrypsin, papain, and nagarse readily hydrolyzed connectin (doublet band of titin) and the band 3 protein (N2-line protein). Pepsin did not attack connectin, but digested the band 3 protein and myosin. Calcium-activated neutral proteinase hydrolyzed the band 3 protein, leaving connectin intact. On the other hand, serine protease digested connectin but not the band 3 protein.

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Year:  1981        PMID: 7026543     DOI: 10.1093/oxfordjournals.jbchem.a133250

Source DB:  PubMed          Journal:  J Biochem        ISSN: 0021-924X            Impact factor:   3.387


  2 in total

1.  Is Nebulin the Product of Duchenne Muscular Dystrophy Gene?

Authors:  Hideo Sugita; Ikuya Nonaka; Yoshiharu Itoh; Atsushi Asakura; Di Hua Hu; Sumiko Kimura; Koscak Maruyama
Journal:  Proc Jpn Acad Ser B Phys Biol Sci       Date:  1987       Impact factor: 3.493

2.  Ultrastructural localization of calcium in post-mortem bovine muscle: a cytochemical and X-ray microanalytical study.

Authors:  X Vignon; J Beaulaton; A Ouali
Journal:  Histochem J       Date:  1989-07
  2 in total

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