Characterization of human carbonic anhydrase III from skeletal muscle

1979 ◽  
Vol 17 (9-10) ◽  
pp. 837-854 ◽  
Author(s):  
Nicholas Carter ◽  
Stephen Jeffery ◽  
Alan Shiels ◽  
Yvonne Edwards ◽  
Terry Tipler ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

Production and Characterization of Monoclonal Antibodies to Human Carbonic Anhydrase III

Hybridoma ◽  
1998 ◽  
Vol 17 (6) ◽  
pp. 553-558 ◽  
Author(s):  
HASSAN M.E. AZZAZY ◽  
PATRICK J. CUMMINGS ◽  
DAVID R. AMBROZAK ◽  
ROBERT H. CHRISTENSON
Keyword(s):  
Monoclonal Antibodies ◽  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

scholarly journals Metabolic and contractile influence of carbonic anhydrase III in skeletal muscle is age dependent

1999 ◽  
Vol 276 (2) ◽  
pp. R559-R565 ◽  
Author(s):  
Claude H. Côté ◽  
Fabrisia Ambrosio ◽  
Guylaine Perreault
Keyword(s):  
Skeletal Muscle ◽  
Data Analysis ◽  
Carbonic Anhydrase ◽  
Soleus Muscle ◽  
Type I ◽  
Carbonic Anhydrase Iii ◽  
Age Dependent ◽  
Old Rats ◽  
Birth Data

Carbonic anhydrase (CA) III is very abundant in type I skeletal muscle, but its function is still debated. Our aims were to examine CA III expression during growth and determine whether the effects of CA inhibition previously observed in adult muscles could be seen in younger rats in which CA III levels are lower. CA III content and activity were measured in soleus muscles from 10- to 100-day-old rats, and the influence of CA inhibitor on fatigue and hexosemonophosphate content was quantified in vitro. CA III activity and content increased fivefold between 10 and 100 days of age. Data analysis revealed that the influence of CA inhibitor on fatigue was to some extent positively and linearly related to the level of CA III activity. Hexosemonophosphate accumulation with CA inhibition also became more significant with age. In conclusion, CA III level in soleus muscle does not stabilize before 3 mo after birth; data also confirm that the effects of CA inhibitors are due to inhibition of the CA III isoform.

Interaction and influence of phenylalanine-198 and threonine-199 on catalysis by human carbonic anhydrase III

Biochemistry ◽  
1993 ◽  
Vol 32 (31) ◽  
pp. 7861-7865 ◽  
Author(s):  
Xian Chen ◽  
Chingkuang Tu ◽  
Philip V. LoGrasso ◽  
Philip J. Laipis ◽  
David N. Silverman
Keyword(s):  
Carbonic Anhydrase ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

scholarly journals Carbonic anhydrase III in skeletal muscle fibers: an immunocytochemical and biochemical study.

1988 ◽  
Vol 36 (7) ◽  
pp. 775-782 ◽  
Author(s):  
P Frémont ◽  
P M Charest ◽  
C Côté ◽  
P A Rogers
Keyword(s):  
Skeletal Muscle ◽  
Carbonic Anhydrase ◽  
Vastus Lateralis ◽  
Muscle Fibers ◽  
Water Soluble ◽  
Type I ◽  
Fiber Types ◽  
Thin Sections ◽  
Carbonic Anhydrase Iii ◽  
Skeletal Muscle Fibers

The objectives of the present study were to determine if carbonic anhydrase III (CA III) demonstrated a specific association for any particular organelle or structure of the skeletal muscle cell and to quantify the activity and content of this enzyme in different types of skeletal muscle fibers. Ultrastructural localization of CA III in the soleus (SOL), deep vastus lateralis (DVL), and superficial vastus lateralis (SVL), composed of predominantly type I, IIa, and IIb fibers, respectively, was performed using a high-resolution immunocytochemical technique and antibody specific for CA III on ultra-thin sections of skeletal muscle embedded in the water-soluble medium polyvinyl alcohol (PVA). The results indicated a uniform distribution of CA III within the sarcomere. Mitochondria, nuclei, triads, Z-, and M-bands were not specifically labeled. Immunoblotting of washed myofibril preparations did not show any detectable CA III associated with this structure. In addition to quantification of the immunogold labeling, CA III activity and content were assayed in the post-mitochondrial supernatant of the three muscles. In the SOL, these values were found to be 3.6-7.6 times higher than in the DVL. The SVL showed a labeling intensity slightly higher than background level, while the enzyme activity and content were indistinguishable from background levels. We therefore conclude that CA III is randomly distributed in the cytoplasm of the three muscle fiber types and that the relative CA III content and activity in the three muscles studied is SOL greater than DVL greater than SVL approximately equal to 0.

Structural and kinetic analysis of proton shuttle residues in the active site of human carbonic anhydrase III

2007 ◽  
Vol 68 (1) ◽  
pp. 337-343 ◽  
Author(s):  
Ileana Elder ◽  
Zoë Fisher ◽  
Philip J. Laipis ◽  
Chingkuang Tu ◽  
Robert McKenna ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Kinetic Analysis ◽  
Active Site ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

Enhancement of the catalytic properties of human carbonic anhydrase III by site-directed mutagenesis

Biochemistry ◽  
1991 ◽  
Vol 30 (6) ◽  
pp. 1484-1490 ◽  
Author(s):  
David A. Jewell ◽  
Chingkuang Tu ◽  
Shanthi R. Paranawithana ◽  
Susan M. Tanhauser ◽  
Philip V. LoGrasso ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Catalytic Properties ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Carbonic Anhydrase Iii ◽  
Human Carbonic Anhydrase

scholarly journals Synthesis and characterization of phenolic Mannich bases and effects of these compounds on human carbonic anhydrase isozymes I and II

2012 ◽  
Vol 28 (2) ◽  
pp. 337-342 ◽  
Author(s):  
Nurgün Büyükkıdan ◽  
Bülent Büyükkıdan ◽  
Metin Bülbül ◽  
Salih Özer ◽  
Hatice Gonca Yalçın
Keyword(s):  
Carbonic Anhydrase ◽  
Mannich Bases ◽  
Synthesis And Characterization ◽  
Human Carbonic Anhydrase
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