Characterisation of cDNA clones for rat muscle carbonic anhydrase III

1988 ◽  
Vol 8 (5) ◽  
pp. 401-406 ◽  
Author(s):  
C. D. Kelly ◽  
N. D. Carter ◽  
S. Jeffery ◽  
Y. H. Edwards
Keyword(s):  
Sexual Dimorphism ◽  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Cdna Clones ◽  
Mrna Levels ◽  
Northern Blots ◽  
Rat Muscle ◽  
Carbonic Anhydrase Iii

cDNA clones for rat muscle carbonic anhydrase III have been isolated from a λ gt-11 library and sequenced. Comparison with human CAIII cDNA showed about 90% homology to rat. The rat clones were used to estimate mRNA from liver and muscle on Northern blots and showed that the sexual dimorphism of CAIII in rat liver relates to a difference in mRNA levels.

scholarly journals Sexual dimorphism in LEC rat liver: Suppression of carbonic anhydrase III by copper accumulation during hepatocarcinogenesis

2011 ◽  
Vol 32 (2) ◽  
pp. 111-117 ◽  
Author(s):  
Makihiko Kuhara ◽  
Jingshu Wang ◽  
Maria Jolina Flores ◽  
Zhiwei Qiao ◽  
Yukio Koizumi ◽  
...  
Keyword(s):  
Sexual Dimorphism ◽  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Copper Accumulation ◽  
Carbonic Anhydrase Iii

scholarly journals Synthesis of rat muscle carbonic anhydrase III in a cell-free translation system

FEBS Letters ◽  
1982 ◽  
Vol 148 (1) ◽  
pp. 122-126 ◽  
Author(s):  
Alan Shiels ◽  
Ian Phillips ◽  
Stephen Jeffrey ◽  
Elizabeth Shephard ◽  
Nicholas Carter
Keyword(s):  
Carbonic Anhydrase ◽  
Translation System ◽  
Rat Muscle ◽  
Carbonic Anhydrase Iii ◽  
Free Translation ◽  
A Cell

Cloning and pretranslational hormonal regulation of testosterone 16α-hydroxylase (P-45016α) in male rat liver

1988 ◽  
Vol 118 (2) ◽  
pp. 314-320 ◽  
Author(s):  
Anders Ström ◽  
Agneta Mode ◽  
Peter Zaphiropoulos ◽  
Anne-Gerd Nilsson ◽  
Edward Morgan ◽  
...  
Keyword(s):  
Rat Liver ◽  
Hormonal Regulation ◽  
Cdna Sequence ◽  
Male Rat ◽  
Complete Agreement ◽  
Cdna Clones ◽  
Expression Library ◽  
Northern Blots ◽  
Terminal Amino ◽  
Secretory Pattern

Abstract. cDNA clones for P-45016α were isolated from a male liver λgt 11 expression library using antibodies against P-45016α. The clones encompassed 1633 and 1791 bp, respectively. The latter clone contained the whole coding sequence. The 20 deduced NH2-terminal amino acids were identical to those of P-450h and the cDNA sequence was in complete agreement with that of P-450 (M-1). Northern blots showed that P-45016α in the rat liver is pretranslationally regulated by the growth hormone secretory pattern. Southern blots indicated that few genes belong to the same P-450 gene family as P-45016α.

Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions

1991 ◽  
Vol 284 (2) ◽  
pp. 270-278 ◽  
Author(s):  
Yuh-Cherng Chai ◽  
Che-Hun Jung ◽  
Chong-Kuei Lii ◽  
Syed S. Ashraf ◽  
Suzanne Hendrich ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Liver Protein ◽  
Carbonic Anhydrase Iii

Identification of an abundant, S-thiolated rat liver protein as carbonic anhydrase III; Characterization of S-thiolation and dethiolation reaction

1990 ◽  
Vol 9 ◽  
pp. 90
Author(s):  
Che-Hun Jung ◽  
Yuh-Cherng Chai ◽  
Chong-Kuei Lii ◽  
Syed S. Ashraf ◽  
Suzanne Hendrich ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Rat Liver ◽  
Liver Protein ◽  
Carbonic Anhydrase Iii

scholarly journals Thyroidectomy significantly alters carbonic anhydrase III concentration and fiber distribution in rat muscle.

1987 ◽  
Vol 35 (6) ◽  
pp. 663-668 ◽  
Author(s):  
S Jeffery ◽  
N D Carter ◽  
A Smith
Keyword(s):  
Carbonic Anhydrase ◽  
Type I ◽  
Fiber Distribution ◽  
Normal Muscle ◽  
Dramatic Effect ◽  
Rat Muscle ◽  
Carbonic Anhydrase Iii ◽  
Type I Fibers ◽  
Atpase Staining

Thyroidectomy has a dramatic effect on rat muscle, greatly increasing the number of Type I fibers and the concentrations of carbonic anhydrase III (CAIII) in the muscle. Carbonic anhydrase III is not confined to the Type I fibers, as was previously believed, but also occurs in fibers that exhibit a level of ATPase staining less than that of 2A fibers but greater than 2B. These fibers are rare in normal muscle but become numerous after thyroidectomy, when they stain heavily for CAIII.

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