Literature DB >> 2730663

Primary structure of rat brain protein carboxyl methyltransferase deduced from cDNA sequence.

M Sato1, T Yoshida, S Tuboi.   

Abstract

Two cDNA clones for protein carboxyl methyltransferase were isolated from a rat brain cDNA library in lambda gt 11 with synthetic oligonucleotides as probes. The two clones differ in size, but the nucleotide sequence including the whole coding region of the shorter cDNA is completely identical with the corresponding sequence of the longer cDNA. The open reading frame encodes a polypeptide of 227 amino acid residues, with a molecular weight of 24,626. This molecular weight is comparable to those reported for other protein carboxyl methyltransferases from several animals, which were determined by gel filtration chromatography or sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

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Year:  1989        PMID: 2730663     DOI: 10.1016/0006-291x(89)91602-1

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

Review 1.  Protein damage and methylation-mediated repair in the erythrocyte.

Authors:  P Galletti; D Ingrosso; C Manna; G Clemente; V Zappia
Journal:  Biochem J       Date:  1995-03-01       Impact factor: 3.857

2.  Automethylation of protein (D-aspartyl/L-isoaspartyl) carboxyl methyltransferase, a response to enzyme aging.

Authors:  J A Lindquist; P N McFadden
Journal:  J Protein Chem       Date:  1994-01

3.  Immunochemical characterization of L-isoaspartyl-protein carboxyl methyltransferase from mammalian tissues.

Authors:  D Boivin; D Bilodeau; R Béliveau
Journal:  Biochem J       Date:  1995-08-01       Impact factor: 3.857

4.  New nucleotide sequence data on the EMBL File Server.

Authors: 
Journal:  Nucleic Acids Res       Date:  1989-09-25       Impact factor: 16.971

  4 in total

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