Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

Analysis of the multiple forms of the 20,000-dalton myosin light, chain from uterine arterial smooth muscles

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:6992006

2D gel electrophoresis resolved the light chain (LC) in four spots, three spots were phosphorylated. Phosphorylation was determined by densitometry (S) and (/sup 32/P)phosphate incorporation (P). Molar (/sup 32/P)phosphate incorporation was quantitated for each LC spot. Phosphorylation was low in resting or drug-relaxed muscles and high in contracting or stretched muscles. At low phosphorylation S > P, this discrepancy can be explained by the presence of unphosphorylated isoforms in the phosphorylated spots. Indeed, unphosphorylated uterine LC exhibited three spots on electrophoretograms (distribution: 0, 13, 7, 80%), whereas arterial LC showed two spots (0, 15, 0, 85%). At high phosphorylation P > S, this aberration is caused by diphosphorylation. In the intact tissue of uterus, the ratio of Thr-P to Ser-P, and the level of diphosphorylation are higher than in artery. The molecular weight and isoelectric points of uterine and arterial LC are the same, but the percentage distribution of the unphosphorylated isoforms, the molar phosphate incorporation in the phosphorylated spots, and the extent of diphosphorylation are different.

Research Organization:
Univ. of Illinois, Chicago
OSTI ID:
6992006
Report Number(s):
CONF-8604222-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Vol. 45:4; ISSN FEPRA
Country of Publication:
United States
Language:
English