Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.24.27 (thermolysin)
 1,894 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A pea chloroplast protein resembles vertebrate and algal actins by several chemical and immunological criteria. On two-dimensional polyacrylamide gels it migrated with a slightly lower relative molecular mass (Mr = 41,000) and slightly more basic isoelectric point than rabbit skeletal muscle actin. A monoclonal antibody to chicken gizzard actin reacted on immunoblots with rabbit skeletal actin, with Chara actin and with a 41,000 Mr band from pea chloroplasts. Pea and Chara bands of approximately 58,000 Mr were also stained. A DNase I-affinity column that bound muscle actin also bound 41,000 and 58,000 Mr chloroplast polypeptides. Similarities existed between enzymically and chemically generated fragments of the 41,000 Mr chloroplast polypeptide and rabbit muscle actin. The 41,000 Mr protein was protected from degradation by thermolysin only in preparations of intact, but not ruptured, isolated chloroplasts, indicating that this protein resides within the outer envelope membrane of these organelles. It is concluded that a 41,000 Mr protein with major similarities to actin occurs inside pea chloroplasts, and that a 58,000 Mr protein with some similarities to actin also probably exists within chloroplasts.
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PMID:An actin-related protein inside pea chloroplasts. 342 94

An isoactin analysis was performed on L-[35S]cysteine labeled BC3H1 cells to determine if these smooth muscle-like cells synthesize vascular smooth muscle actin. Three different NH2-terminal peptides were identified on thin layer electrophoretograms of DNase I-purified and trypsin-digested BC3H1 cell actin. Results obtained from secondary digestion with thermolysin or Staphylococcus aureus V8 protease showed that the most acidic NH2-terminal peptide was derived from vascular smooth muscle alpha-isoactin. Treatment of cell monolayers with serum-free medium caused a 3-fold increase in the level of alpha-isoactin expression and a concomitant decrease in the level of non-muscle beta- and gamma-isoactin. Cell-cell contact was required for induction of alpha-isoactin, and the effects of serum depletion on isoactin expression and cell growth were reversible. The intensity of about 11 out of 500 polypeptide spots on two-dimensional gels of BC3H1 cell polypeptides also was influenced by the culture conditions. The finding that smooth muscle isoactin expression was coupled to cell growth conditions indicate the potential usefulness of BC3H1 cells in studies of isoactin expression and utilization during vascular smooth muscle development.
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PMID:Induction of vascular smooth muscle alpha-isoactin expression in BC3H1 cells. 669 10