These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Structural difference between alpha-paramyosin and beta-paramyosin of Mercenaria mercenaria.
    Author: Yeung AT, Cowgill RW.
    Journal: Biochemistry; 1976 Oct 19; 15(21):4654-9. PubMed ID: 974083.
    Abstract:
    A method is described for extraction of alpha-paramyosin in amounts comparable to that formerly attained for beta-paramyosin (15-25 mg/g of muscle). A modification of the procedure for sodium dodecyl sulfate gel electrophoresis is described that permits the separation on coelectrophoresis of alpha-paramyosin (207 000 daltons) and beta-paramyosin (200 000 daltons). The alpha- and beta-paramyosins also can be distinguished by gel electrophoresis at pH 2.3 and by differences in solubility in the region of 0.2-0.4 ionic strength at neutral pH. Evidence is presented that the segment lost from alpha-paramyosin during degradation to beta-paramyosin came from the C-terminal end. This evidence is based on determinations of N- and C-terminal amino acids and on the size of segments obtained after chemical cleavage at the sites of Cys residues. It has been observed earlier that the solubility characteristics of beta-paramyosin at neutral pH are determined by the C-terminal one-third of the molecule and the present results indicate that the additional small segment of about 3.5% of the total mass that is present in the C-terminal end of alpha-paramyosin accounts for the marked difference in solubility of the two forms.
    [Abstract] [Full Text] [Related] [New Search]