Literature DB >> 1397316

p33, an endogenous target protein for arginine-specific ADP-ribosyltransferase in chicken polymorphonuclear leukocytes, is highly homologous to mim-1 protein (myb-induced myeloid protein-1).

K Yamada1, M Tsuchiya, K Mishima, M Shimoyama.   

Abstract

We have determined the partial amino acid sequence of p33, an endogenous substrate protein for arginine-specific ADP-ribosyltransferase in chicken polymorphonuclear leukocytes (heterophils), and found that the sequence was completely identical with the regions of amino acid sequences deduced from mim-1 (named for myb-induced myeloid protein-1, which is expressed in chicken promyelocytes) cDNA [(1989) Cell, 59, 1115-1125], except for one amino acid difference (Tyr297-->Ile). These results together with data on cellular and subcellular distributions of p33 in heterophils suggest that mim-1 may encode the precursor protein of p33.

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Year:  1992        PMID: 1397316     DOI: 10.1016/0014-5793(92)81102-r

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  2 in total

Review 1.  Target protein for eucaryotic arginine-specific ADP-ribosyltransferase.

Authors:  M Tsuchiya; M Shimoyama
Journal:  Mol Cell Biochem       Date:  1994-09       Impact factor: 3.396

2.  Lipopolysaccharide-induced change of ADP-ribosylation of a cytosolic protein in bone-marrow-derived macrophages.

Authors:  S Hauschildt; P Scheipers; W G Bessler
Journal:  Biochem J       Date:  1994-01-01       Impact factor: 3.857

  2 in total

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