Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.6.4.1 (myosin ATPase)
 1,140 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myosin was isolated from the ventricular myocardium of adult rats and the effect of time, 2-mercaptoethanol and inhibitors of proteases was investigated on its properties. It was found that the storage of cardiac muscle up to 4 hours does not influence the myosin ATPase, the electrophoretic pattern of light chains of myosin or the pattern of peptides produced by digestion of myosin with chymotrypsin. Neither does the presence of pepstatin and phenylmethyl sulfonylfluoride during myosin preparation influence the activity of myosin ATPase. It was found that the presence of 2-mercaptoethanol during myosin preparation enhances myosin ATPase of the product. This myosin was more stable when kept at 4 degrees C for four days.
 ...
PMID:The effect of time, 2-mercaptoethanol and inhibitors of proteases on isolation of cardiac myosin and its properties. 252 75

Limited digestion of calmodulin (CaM)-dependent myosin light chain kinase from turkey gizzard with alpha-chymotrypsin in the presence of bound CaM generated an 80,000-dalton kinase fragment that was fully active in the absence of Ca2+. This kinase catalyzed specific Ca2+-independent phosphorylation of the 20,000-dalton light chain of myosin using isolated light chains, intact myosin, and actomyosin. Phosphorylation of myosin in the absence of Ca2+ allowed us to dissociate myosin phosphorylation from other potential Ca2+-dependent regulatory mechanisms, thus permitting an evaluation of the postulated central role of myosin phosphorylation in the regulation of smooth muscle contraction. Ca2+-independent myosin phosphorylation was found to cause loss of Ca2+ sensitivity of 1) actin-activated myosin ATPase activity in a crude actomyosin preparation, and 2) tension development in skinned smooth muscle fibers in the absence of Ca2+. Myosin phosphorylation is, therefore, the key event in actin activation of ATPase activity and initiation of contraction in skinned chicken gizzard fibers.
 ...
PMID:Gizzard Ca2+-independent myosin light chain kinase: evidence in favor of the phosphorylation theory. 684 77