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Purification and characterization of catabolic dehydroquinase, an enzyme in the inducible quinic acid catabolic pathway of Neurospora crassa
Catabolic dehydroquinase which functions in the inducible quinic acid catabolic pathway in Neurospora crassa has been purified 8000-fold. The enzyme was purified by two methods. One used heat denaturation of contaminating proteins; the other used antibody affinity chromatography. The preparations ob...
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Published in: | The Journal of biological chemistry 1975-08, Vol.250 (15), p.6008-6014 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Catabolic dehydroquinase which functions in the inducible quinic acid catabolic pathway in Neurospora crassa has been purified
8000-fold. The enzyme was purified by two methods. One used heat denaturation of contaminating proteins; the other used antibody
affinity chromatography. The preparations obtained by these two methods were identical by all criteria. The purified enzyme
is extremely resistant to thermal denaturation as well as denaturation 0y urea and guanidine hydrochloride at 25 degrees.
It is irreversibly inactivated, although not efficiently dissociated, by sodium dodecyl sulfate and guanidine hydrochloride
at 55 degrees. At pH 3.0, the enzyme is reversibly dissociated into inactive subunits. At high concentrations catabolic dehydroquinase
aggregates into an inactive, high molecular weight complex. The native enzyme, which has a very high specific activity, has
a molecular weight of approximately 220,000 and is composed of identical subunits of 8,000 to 12,000 molecular weight each.
The native enzyme and the subunit are both asymmetric. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)41150-2 |