o-Iodosobenzoic oxidation and cleavage of myosin subfragment 1.
C Longo, B Garrido, G Zalba, N López-Moratalla, E Santiago
Index: Int. J. Biochem. 24(1) , 133-43, (1992)
Full Text: HTML
Abstract
1. o-Iodosobenzoic acid (IOB) caused the formation of a disulfide bridge between SH1 and SH2 groups of myosin SF1 rendering inactive its ATPase activity. 2. IOB at high concentrations provoked fragmentation of SF1 at its tryptophan residues. 3. The main fragmentation point was located at 15 K from the amino terminus of the myosin heavy chain. 4. Actin was not fragmented by IOB. It protected SF1 tryptophans from IOB attack. 5. These results suggest a possible use of IOB as a reagent to study protein tryptophan under nondenaturing conditions.
Related Compounds
Related Articles:
1991-04-01
[Appl. Environ. Microbiol. 57(4) , 962-8, (1991)]
1987-08-25
[J. Biol. Chem. 262(24) , 11714-20, (1987)]
Epitopes of Escherichia coli ribosomal protein S13.
1989-12-01
[J. Protein Chem. 8(6) , 701-17, (1989)]
Influence of the polymer-micelle interaction on micelle-substrate binding.
2010-03-01
[J. Pharm. Sci. 99(3) , 1440-51, (2010)]
1989-01-01
[Int. J. Biochem. 21(5) , 549-54, (1989)]