Structural analysis of mutant Carbonic Anhydrase II from bovine.
نویسندگان
چکیده
منابع مشابه
Periplasmic carbonic anhydrase structural gene (Cah1) mutant in chlamydomonas reinhardtii
To survive in various conditions of CO2 availability, Chlamydomonas reinhardtii shows adaptive changes, such as induction of a CO2-concentrating mechanism, changes in cell organization, and induction of several genes, including a periplasmic carbonic anhydrase (pCA1) encoded by Cah1. Among a collection of insertionally generated mutants, a mutant has been isolated that showed no pCA1 protein an...
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Carbonic anhydrase II (CA II) deficiency is an extremely rare autosomal recessive disorder, characterised by a triad of osteopetrosis, renal tubular acidosis and cerebral calcifications. A 12 year old boy with classical features of CA II deficiency is reported who was found to be homozygous for the mutation in CA II gene and parents were heterozygous for the same mutation .To the best of our kn...
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The temperature dependence of the activity and structure of the enzyme carbonic anhydrase was studied. The Arrhenius plot shows a jump which is seen usually in proteins with more than one subunit or with one subunit but more than one domain. Since carbonic anhydrase has only one subunit with one domain, the fine conformational changes of the protein motifs could only be detected through circula...
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The denaturation and renaturation of bovine carbonic anhydrase B is a thermodynamically reversible process, uncomplicated by aggregation or disuhide bond formation. The reaction is less cooperative than is the unfolding and refolding of most globular proteins, in that distinct successive stages can be observed both in equilibrium and kinetic measurements. This enzyme is therefore ideally suited...
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Bromoacetazolamide effects rather quickly a partial, and more slowly an almost complete, irreversible inactivation of bovine carbonic anhydrase B (EC 4.2.1.1). Under identical conditions, the enzyme is not inactivated by bromoacetic acid or iodoacetamide, nor does it react significantly with these compounds. The zinc-free enzyme does not undergo irreversible binding with W-bromoacetazolamide an...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2001
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.41.s37_1