Purification and Properties of an Avian Carbonic Anhydrase from the Erythrocytes of Gallus domesticus

Bernstein, Robert S.; Schraer, Rosemary

doi:10.1016/s0021-9258(19)45647-0

Cited by 65 publications

References 58 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Ultrastructural immunocytochemical localization of carbonic anhydrase in normal and calcitonin‐treated chick osteoclasts

Anderson¹,

Schraer²,

Gay³

1982

Anat. Rec.

View full text Add to dashboard Cite

Carbonic anhydrase was localized in osteoclasts by light and electron microscopy using a preembedding peroxidase-antiperoxidase staining method. Osteoclasts on the endosteal surface of the metatarsi of calcitonin-treated and untreated (control) chicks were studied. A positive staining reaction was seen in the cytosol, in the Golgi apparatus, in and on vesicles, on the plasma membrane of the ruffled border, and on the bone surface beneath control osteoclasts. After calcitonin treatment, positive staining reactions were seen at the same sites except that staining was absent on the plasma membrane and endosteal bone surface. The morphology of osteoclasts from calcitonin-treated chicks was indicative of cell inactivity. The carbonic anhydrase which was bound to the plasma membrane of the ruffled border is appropriately arrayed for hydrogen ion secretion and subsequent mineral dissolution. The presence of the enzyme within lysosomelike vesicles and on the endosteal surface beneath active cells suggests that it may be released into the resorbing zone along with the lysosomal hydrolases. The function of the extracellular enzyme is also unknown.

show abstract

Ultrastructural immunocytochemical localization of carbonic anhydrase in normal and calcitonin‐treated chick osteoclasts

Anderson¹,

Schraer²,

Gay³

1982

Anat. Rec.

View full text Add to dashboard Cite

show abstract

Mammalian carbonic anhydrase isozymes : Evidence for A third locus

Holmes

1976

J. Exp. Zool.

View full text Add to dashboard Cite

Starch gel electrophoretic patterns of carbonic anhydrase (CA) isozymes were examined from tissue extracts of sheep, mice, rabbits, and chickens. In addition to the widely distributed and extensively studied B and C isozymes, an additional isozyme (called CA-A) was observed, which was predominantly localized in muscle tissue. Immunochemical studies showed the A isozyme to be homologous with CA-B. Developmental and tissue distribution analyses suggested that a third locus (A) is involved in carbonic anhydrase synthesis in mammals.

show abstract

Listing of Protein Spectra

Kirschenbaum

1984

Bibliographic Atlas of Protein Spectra in the Ultraviolet and Visible Regions

View full text Add to dashboard Cite

Purification and Properties of an Avian Carbonic Anhydrase from the Erythrocytes of Gallus domesticus

Cited by 65 publications

References 58 publications

Ultrastructural immunocytochemical localization of carbonic anhydrase in normal and calcitonin‐treated chick osteoclasts

Ultrastructural immunocytochemical localization of carbonic anhydrase in normal and calcitonin‐treated chick osteoclasts

Mammalian carbonic anhydrase isozymes : Evidence for A third locus

Listing of Protein Spectra

Contact Info

Product

Resources

About