English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Plus monthly

Global: Zendy Tools annual

Global: Zendy Tools monthly

Global: Zendy Free Plan

The amino-acid sequence of the short subfragment-2 in the amino-terminal portion of subfragment-2 derived from adult chicken ventricular muscle myosin was completely determined by direct protein analysis. Peptides fragmented by cyanogen bromide, lysyl endopeptidase and arginyl endopeptidase of S-carboxymethylated S-2 and peptides of large CNBr peptides cleaved by dilute formic acid were separated and sequenced. This short S-2 composed of 259 amino-acid residues was found highly conserved and contained hydrophobic and charged residue repeat units. Comparing this sequence with the partial nucleotide sequence of cDNA corresponding to short S-2 (Stewart A.F.R., et al. (1991) J. Mol. Evol. 33, 357-366), a 64 amino-acid residues extension towards the NH2 terminus and 9 residues differences were observed. Furthermore, this sequence is compared with those of rat, rabbit and human ventricular myosins, and 86.1%, 86.5%, 86.5% sequence identities are observed, respectively.

Amino-Acid Sequence of the Short Subfragment-2 in Adult Chicken Cardiac Muscle Myosin