Role of myosin heavy chains from rabbit skeletal muscle in the heat-induced gelation mechanism

Autor:	Hiroshi Yamauchi, Ali Asghar, Tsutomu Yasui, Kunihiko Samejima
Rok vydání:	1984
Předmět:	animal structures Myosin light-chain kinase Chemistry Ionic bonding Skeletal muscle General Biochemistry Genetics and Molecular Biology Random coil Myosin head medicine.anatomical_structure Biochemistry Ionic strength Myosin medicine Solubility General Agricultural and Biological Sciences
Zdroj:	Agricultural and Biological Chemistry. 48:2225-2232
ISSN:	1881-1280 0002-1369
DOI:	10.1271/bbb1961.48.2225
Popis:	Some physico-chemical and heat-induced gelling properties of myosin heavy chains (MHCs) from rabbit skeletal muscle were studied. MHCs were found to be almost devoid of ATPase activity, possibly because of the absence of myosin light chains. MHCs formed precipitates below and ionic strength of 0.3, and above this ionic strength MHCs became soluble. On heating to 65°C at low concentrations of the protein, MHCs lost their solubility and formed aggregates even at high ionic conditions. Partially irreversible change in the conformation of MHC (from helical to random coil) also occurred in heated MHCs.The heat-induced gel strength of MHCs was found to be almost equal to that of intact myosin molecules with identical protein concentrations. This suggests that the gelling potential of myosin is solely confined in MHC. Although myosin light chains do not seem to contribute to the gelling power of myosin, possibly they provide some stability to the gel if the pH is varied above the optimum value, i.e., 6.0. The ad...
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9cf2be2d32bb37d2da6fb13d3046f353 https://doi.org/10.1271/bbb1961.48.2225 Zobrazit plný text záznamu