Abstract:
:A monoclonal antibody (MF5), capable of recognizing a divalent cation-induced conformational change in myosin light chain 2 (LC2f), has been used to screen a cDNA library constructed in the expression vector lambda gt11. A clone has been isolated that contains the whole coding sequence of this myosin subunit. The light chain was synthesized as a fusion peptide linked to beta-galactosidase by ten amino acids encoded in the 5' untranslated region of its mRNA. Seven imperfect repeats were identified in the 3' untranslated region of the mRNA. The amino acids conferring specificity on the MF 5 epitope were established by first determining the nucleotide sequence of shorter subclones that expressed the epitope and then eliminating those amino acid residues shared by cardiac myosin LC2, which was unreactive with this antibody. The epitope, which becomes accessible to MF 5 upon removal of bound divalent cations, resides at the junction between the first alpha-helical domain and the metal binding site. Theoretically, this approach can be used to define the primary structure of most protein epitopes.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Reinach FC,Fischman DAdoi
10.1016/0022-2836(85)90229-3subject
Has Abstractpub_date
1985-02-05 00:00:00pages
411-22issue
3eissn
0022-2836issn
1089-8638pii
0022-2836(85)90229-3journal_volume
181pub_type
杂志文章abstract::The structure of replicating simian virus 40 (SV40) minichromosomes was studied by DNA crosslinking with trimethyl-psoralen. The procedure was used both in vitro with extracted SV40 minichromosomes as well as in vivo with SV40-infected cells. Both procedures gave essentially the same results. Mature SV40 minichromosom...
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pub_type: 杂志文章
doi:10.1016/j.jmb.2006.08.072
更新日期:2006-11-17 00:00:00
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journal_title:Journal of molecular biology
pub_type: 杂志文章
doi:10.1016/j.jmb.2006.05.032
更新日期:2006-07-14 00:00:00
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pub_type: 杂志文章
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journal_title:Journal of molecular biology
pub_type: 杂志文章
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