A comparative electrophoretic analysis of mammalian carbonic anhydrase isozymes: Evidence for a third isozyme in red skeletal muscles

Holmes, Roger S.

doi:10.1016/0305-0491(77)90159-6

Search citation statements

Order By: Relevance

Paper Sections

Select...

Calli1

Discussion1

Citation Types

Supporting

Mentioning

Contrasting

Year Published

1978

2015

Publication Types

Select...

Article4

Book2

Relationship

Self Cite0

Independent6

Authors

Journals

Cited by 9 publications

(2 citation statements)

References 14 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…CA III was first detected in skeletal muscle (Holmes, 1977;Koester et aI., 1977). It has since been identified as the predominant cytosolic protein of skeletal muscle (Geers and Gros, 1991) and adipose tissue (Lynch et aI., 1993).…”

Section: Callimentioning

confidence: 99%

The catalytic mechanism of mammalian carbonic anhydrases

Lindskog

Silverman

2000

The Carbonic Anhydrases

View full text Add to dashboard Cite

Section: Callimentioning

confidence: 99%

The catalytic mechanism of mammalian carbonic anhydrases

Lindskog

Silverman

2000

The Carbonic Anhydrases

View full text Add to dashboard Cite

“…In particular CA-I and CA-II in erythrocytes [1][2][3][4], and CA-III in skeletal muscle [5][6][7][8], have been purified, extensively investigated, and fully characterized. Human muscle CA-III has been thought to be distinguished from human erythrocyte CA isozymes in regard to its immunological and biological characteristics.…”

Section: Discussionmentioning

confidence: 99%

Presence of carbonic anhydrase III in erythrocyte.

Ohta

Nishitani

et al. 1990

J. Clin. Biochem. Nutr.

View full text Add to dashboard Cite

Characterization of human carbonic anhydrase III from skeletal muscle

et al. 1979

View full text Add to dashboard Cite

A third form of human carbonic anhydrase (CA III), found at high concentrations in skeletal muscle, has been purified and characterized. This isozyme shows relatively poor hydratase and esterase activities compared to the red cell isozymes, CA I and CA II, but is similar to these isozymes in subunit structure (monomer) and molecular size (28,000). CA III is liable to posttranslational modification by thiol group interaction. Monomeric secondary isozymes, sensitive to beta-mercaptoethanol, are found in both crude and purified material and can be generated in vitro by the addition of thiol reagents. Active dimeric isozymes, generated apparently by the formation of intermolecular disulfide bridges, also occur but account for only a small proportion of the total protein and appear only when the concentration of CA III is particularly high.

show abstract

A comparative electrophoretic analysis of mammalian carbonic anhydrase isozymes: Evidence for a third isozyme in red skeletal muscles

Cited by 9 publications

References 14 publications

The catalytic mechanism of mammalian carbonic anhydrases

The catalytic mechanism of mammalian carbonic anhydrases

Presence of carbonic anhydrase III in erythrocyte.

Characterization of human carbonic anhydrase III from skeletal muscle

Contact Info

Product

Resources

About