cDNA cloning of pig testicular lactate dehydrogenase-C, thermal stability of the expressed enzyme, and polymorphism among strains

Authors
Huang, HW Liu, TZ Lee, KH Tu, CF Lee, WC Shimogiri, T Mannen, H Li, SSL
Citation
Hw. Huang et al., cDNA cloning of pig testicular lactate dehydrogenase-C, thermal stability of the expressed enzyme, and polymorphism among strains, GENE, 242(1-2), 2000, pp. 151-154
Citations number
10
Categorie Soggetti
Molecular Biology & Genetics
Journal title
GENE
ISSN journal
03781119 → ACNP
Volume
242
Issue
1-2
Year of publication
2000
Pages
151 - 154
Database
ISI
SICI code
0378-1119(20000125)242:1-2<151:CCOPTL>2.0.ZU;2-9
Abstract
Pig testicular lactate dehydrogenase-C (LDHC) cDNA was cloned and sequenced . The deduced sequence of 332 amino acids from pig LDHC shows 73% and 67% i dentity with that of pig LDHA (muscle) and LDHB (heart) respectively, where as pig LDHA and LDHB isozymes shows 74% sequence identity. Pig and mouse LD HC cDNAs were subcloned into bacterial expression vector, and the expressed pig LDHC isozyme was shown to be as thermally stable as mouse LDHC isozyme . Pig genomic DNAs from Chinese Meishan, English Yorkshire, Danish Landrace and American Duroc were shown to exhibit polymorphic sites for restriction enzymes EcoRI, BamHI and PstI. (C) 2000 Elsevier Science B.V. All rights r eserved.