Studies on a Myosin Fragment Obtained by Ammonium Sulphate Treatment of Myosin.
نویسندگان
چکیده
منابع مشابه
Studies on subfragment-I, a biologically active fragment of myosin.
The relationship between the structure and function of the myosin molecule is of considerable importance in the understanding of the molecular mechanism of muscle contraction. The nature of the adenosine triphosphatase (ATPase) site and the subunit structure are of special interest in this respect. The hydrolysis of ATP by myosin appears to link the conversion of chemical energy to the mechanic...
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Objective(s):The objective of this study was to investigate the interaction of daunorubicin (DNR) and cardiac myosin (CM) and the changes in mice hearts to exhibit DNR-induced cardiotoxicity . Materials and Methods:The interaction between DNR and CM was expressed using fluorescence quenching at pH 4.0-9.0 and 15-37 °C. DNR-induced cardiotoxicity was studied using in vivo experiment. Forty grou...
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Partial hydrolysis of human platelet or uterine smooth muscle myosin with insoluble papain yielded rod fragments, insoluble at low ionic strength and devoid of ATPase activity. This protein migrated on sodium dodecyl sulfate-8 M urea gel electrophoresis as a single band with a molecular weight of approximately 110,000 to 120,000 corresponding to the rod portion of myosin. Rabbit antibodies to p...
متن کاملfluorescence spectra of cardiac myosin and in vivo experiment: studies on daunorubicin-induced cardiotoxicity
objective(s):the objective of this study was to investigate the interaction of daunorubicin (dnr) and cardiac myosin (cm) and the changes in mice hearts to exhibit dnr-induced cardiotoxicity . materials and methods:the interaction between dnr and cm was expressed using fluorescence quenching at ph 4.0-9.0 and 15-37 °c. dnr-induced cardiotoxicity was studied using in vivo experiment. forty grou...
متن کاملStudies on the heterogeneity of subfragment-1 preparations. Isolation of a new proteolytic fragment of the heavy chain of myosin.
1. The physical, chemical and enzymic properties of subfragment 1 prepared from myosin of rabbit skeletal muscle by using two different concentrations of insoluble papain were compared. 2. Subfragment 1 prepared by using a myosin/papain ratio of 2000: 1 (by wt.) migrated on electrophoresis in non-dissociating conditions as a single enzymically active band. When prepared with a myosin/papain rat...
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ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1956
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.10-0151c