期刊
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY
卷 138, 期 3, 页码 277-283出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cbpc.2004.04.010
关键词
acylase I; rat kidney; porcine intestine; marathon library; cDNA cloning; sequence; analysis; cysteine; enzyme
A new cDNA form encoding the rat kidney acylase I was characterized and found to show as much as 93.5% identity in its translated nucleotide sequence and, to a lesser extent, in its 3'-untranslated region with the nucleotide sequence we previously reported in 2000. Comparisons between the amino acid sequences of the two corresponding proteins showed the presence of N-terminal fragments with 88.5% identity and different cysteine profiles. The cDNA nucleotide sequence of the pig intestinal enzyme isolated from a marathon library turned out to be 100% identical to that of the kidney enzyme, but differed from those of the two rat kidney acylase I forms. (C) 2004 Elsevier Inc. All rights reserved.
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