Abstract:
:The molecular mechanism of smooth muscle contraction was approached by a novel method, covalent 14C-labeling. Intra- and intermolecular protein interactions during contractile activity are reflected by changed reactivity of protein side chains; these can be detected by reagents which readily permeate through the muscle membrane without affecting the contractility and form covalent bonds with proteins in the muscle. The incorporation of 14CH2ICONH2 into proteins of 1-hour histamine contracted versus resting porcine carotid arterial muscles was determined. Out of fourteen 14C-labeled proteins analyzed, only two showed a change in reactivity during sustained contraction. The incorporation of 14CH2ICONH2 into calponin and caldesmon in contracted muscles was about 66% of that into these same proteins in resting muscles. A transformation of calponin and caldesmon molecules from an extended to a more compact conformation explains the decreased reactivity.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Bárány K,Polyák E,Bárány Mdoi
10.1016/0006-291x(92)91274-tsubject
Has Abstractpub_date
1992-09-16 00:00:00pages
847-52issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(92)91274-Tjournal_volume
187pub_type
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