Photocross-linking from SH1 of the myosin heavy chain to light chains through the dinitrophenyl group attached to SH1.
Trinitrobenzene selectively dinitrophenylates SH1, a specific thiol in the myosin heavy chain which contains 1 mol of this cysteinyl residue. When the SH1-DNP-myosin thus obtained was irradiated with a mercury lamp, a cross-linked product was formed with a molecular weight of about 220K daltons. It was shown that this product was composed of both heavy and light chains by fluorescence labeling of the heavy chain at SH2, another specific thiol, and immune reaction using an anti-light chain antibody, respectively.
D000818:Animals; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D008970:Molecular Weight; D009132:Muscles / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D009578:Nitrobenzenes; D011817:Rabbits; D013438:Sulfhydryl Compounds / Q000032:analysis; D014301:Trinitrobenzenes
D009578:Nitrobenzenes; D013438:Sulfhydryl Compounds; D014301:Trinitrobenzenes; C043308:1,2,4-trinitrobenzene; D009218:Myosins