Two chymotrypsin-susceptible sites of myosin rod from chicken gizzard
نویسندگان
چکیده
منابع مشابه
Isolation of the native form of chicken gizzard myosin light-chain kinase.
A simple and rapid procedure for the purification of the native form of chicken gizzard myosin light-chain kinase (Mr 136000) is described which eliminates problems of proteolysis previously encountered. During this procedure, a calmodulin-binding protein of Mr 141000, which previously co-purified with the myosin light-chain kinase, is removed and shown to be a distinct protein on the basis of ...
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TYPE 1 avian adenoviruses belong to the genus Aviadenovirus within the adenovirus family. Five species of fowl adenovirus (fAdV) (designated by the letters A to E) are recognised within the Aviadenovirus genus based largely on molecular criteria, in particular restriction enzyme fragmentation patterns and sequencing data (McFerran and McConnel Adair 2003). fAdV are common infectious agents in p...
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We have examined the protease susceptibility of aortic myosin, the thermal unfolding profiles of myosin rod and light meromyosin (LMM) and the solubility properties of the LMM fragments. Two major protease-susceptible sites were found, located at the head-rod junction and the heavy meromyosin (HMM)-LMM junction. Both tryptic and chymotryptic digestion of aortic myosin rod produced the LMM (80-8...
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Introduction Myosin is the major structural and functional protein in skeletal muscle fibers. Myosin contains an actin-activated ATPase activity that is the driving force for the relative shortening of the myofibril and is responsible for force generation in skeletal muscle (10). Within the myofibril, myosin is found within a structure known as a thick filament. Native thick filaments isolated ...
متن کاملStudies on the soluble phosphodiesterases of chicken gizzard smooth muscle.
In this study we describe the identification of four soluble forms of cyclic nucleotide phosphodiesterase from chicken gizzard smooth muscle. These isoenzymes were separated from one another by ion-exchange chromatography on DEAE-cellulose and by calmodulin-Sepharose affinity chromatography. Each form migrates as a single discrete band when it is electrophoresed on non-denaturing polyacrylamide...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1985
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1985.tb08870.x