In:
European Journal of Biochemistry, Wiley, Vol. 227, No. 1-2 ( 1995-01), p. 459-465
Abstract:
Porcine aorta myosin was reacted with a bifunctional cross‐linking reagent, N,N ′‐ o ‐phenylenedimaleimide. The 17‐kDa essential light chain (LC17) in each myosin head was intramolecularly cross‐linked within a single myosin molecule. The 34‐kDa cross‐linked LC17 dimer was isolated and its peptide map, after lysylendopeptidase digestion, was obtained by reverse‐phase HPLC. Based on the amino acid compositions of peptide fragments, the N‐terminal Cys residues of LC17 subunits were assigned to be cross‐linked to each other. To study the distribution of two LC17 isoforms, LC17nm and LC17gi [Hasegawa, Y., Ueda, Y., Watanabe, M. & Morita, F. (1992) J. Biochem. 111 , 798–803], aorta myosin was reacted with 5,5′‐dithiobis(2‐nitrobenzoic acid) (Nbs 2 ). The LC17 dimer cross‐linked with Nbs 2 was resolved into three distinct bands on urea/PAGE using a 4% acrylamide gel. Densitometric analysis of the three band intensities showed that three pairs of LC17 isoforms in aorta myosin are present in the ratio of LC17nm‐LC17nm/LC17nm‐LC17gi/C17gi‐LC17gi = 22:46:32. This ratio is consistent with the random combination of two LC17 isoforms with myosin heavy chains.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1995.227.issue-1-2
DOI:
10.1111/j.1432-1033.1995.tb20410.x
Language:
English
Publisher:
Wiley
Publication Date:
1995
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
2172518-4
SSG:
12
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