Testosterone‐induced, sulfonamide‐resistant carbonic anhydrase isozyme of rat liver is indistinguishable from skeletal muscle carbonic anhydrase III

Carter, Nicholas D.; Hewett‐Emmett, David; Jeffrey, Steve; Tashian, Richard E.

doi:10.1016/0014-5793(81)81094-0

Cited by 89 publications

(38 citation statements)

References 16 publications

(2 reference statements)

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“…The evidence for a single structure gene locus coding CA111 in most rat tissues is strong [9], and the variable expression of this locus in different muscle types and in male vs female liver is established by these data. If we compare male liver with female liver and soleus muscle (red, slow) with EDL (fast, white) muscle, the CA111 level is -30~times higher in the former tissue of each pair (tig.2).…”

Section: Diissionmentioning

confidence: 79%

“…It now appears that high levels of a CA111 isozyme structurally indistinguishable from rat muscle CAR1 are also present in mature rat liver [9]. Utilizing an electrophoretic immunoassay [8] we report here the levels of CA111 in different rat tissues.…”

Section: Introduction 22 Immunoassaymentioning

confidence: 99%

“…Relatively high levels (i.e., up to 1% wet muscle wt) of a low-activity sulfonamide-resistant carbonic anhydrase isozyme has been reported from skeletal muscle of chicken, cat and sheep [ 11, ox [2], rabbit [3], mouse [4], human [8,9] and gorilla [7]. It has been accepted that these isozymes are all homologous forms of an enzyme designated CA111 and essentially confined to skeletal muscle.…”

Section: Introduction 22 Immunoassaymentioning

confidence: 99%

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Immunoassay of carbonic anhydrase III in rat tissues

1982

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Section: Diissionmentioning

confidence: 79%

Section: Introduction 22 Immunoassaymentioning

confidence: 99%

Section: Introduction 22 Immunoassaymentioning

confidence: 99%

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Immunoassay of carbonic anhydrase III in rat tissues

1982

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“…Recently, it was shown [6] that rat muscle isoenzyme III is identical with the 'sulfonamide-resistant' carbonic anhydrase discovered in lper of male rats . The amino acid sequence of bovine carbonic anhydrase III has been reported [lo].…”

Section: Cobalt(ii)mentioning

confidence: 99%

Effects of pH and inhibitors on the absorption spectrum of cobalt(II)‐substituted carbonic anhydrase III from bovine skeletal muscle

Engberg¹,

Lindskog²

1984

FEBS Letters

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Bovine apocarbonic anhydrase III has been prepared by incubation with 2-c~boxy-l,lO-phenanthroIine at pH 5.5, The Co(II)-substituted enzyme has been prepared and its absorption spectrum has been studied. The spectrum is nearly pH-independent above pH 6. It is very similar to the high pH spectral forms of Co(II)-carbonic anhydrases I and II. The spectra of complexes with the sulfonamide inhibitor, acetazolamide, and with CN-and NCO-are virtually identical to the spectra of the corresponding complexes with Co(II)-isoenzymes I and II. The spectrum of the NS complex indicates that this anion is bound somewhat differently in Co(H) isoenzyme III than in the other Co(II)-substituted isoenzymes. Carbonic anhydrase Isoenzyme Muscle

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“…The, very low-activity isozyme, CA-III was discovered in skeletal muscle and male rat liver, and shown to be present in myoepithelial cells of the uterus, prostate, mammary glands of humans, and ductal cells of the salivary glands of rats, hamster, cows and horses Asari et al, 1989). Carbonic anhydrase III is particularly resistant to inhibition by acetazolamide (Armstrong et al, 1966;Carter et al, 1981;Deutsch, 1987;Tashian, 1989).…”

mentioning

confidence: 99%