Journal
JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
Volume 50, Issue 1, Pages 196-202Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jf010727m
Keywords
myosin; denaturation; aggregation; gelation; carp
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Carp dorsal myosin formed oligomers that retained ATPase activity upon heating. Cleavage of the oligomeric myosin at subfragment-1 (S-1)/rod junction released monomeric S-1 and rod, indicating that ATPase retaining myosin associated near the S-1/rod junction. The digest also contained rod oligomers. Heating a mixture of S-1 and rod generated neither ATPase retaining S-1 oligomers nor rod oligomers. Electron microscopic observation of the heated myosin revealed that some oligomers were formed by associating at the S-1/rod joining region, exhibiting a recognized double head, probably ATPase retaining oligomers. No myosin oligomers associated at the tail region were observed, thus, rod aggregation would be formed at its very restricted region near the S-1 /rod junction. Based on the findings, we proposed that the neck structure is important in the thermal oligomerization process of myosin.
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