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The biological function of the R2a regulatory gene for alkaline phosphatase in Escherichia coli |
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| Authors: | S Kida |
| Institution: | 1. Department of Pathology and Center for Research in Oral Biology, University of Washington Medical School, Seattle, Washington, U.S.A.;2. Departments of Orthopedic Surgery and Medicine, University of California at San Francisco, San Francisco, California, U.S.A.;3. Laboratory of Biochemistry, National Institute of Denial Research, NIH, Bethesda, Maryland 20014, U.S.A. |
| Abstract: | Previous attempts to purify lysyl oxidase have been frustrated by the failure to recover activity during ion exchange or affinity chromatography. We have found that lysyl oxidase from chick cartilage shows marked stability in buffers containing urea and in these solutions can be recovered in high yield from DKAE-cellulose and collagen-derivatized Sepharose. The purified enzyme was active against both collagen and elastin substrates but devoid of monoamine oxidase activity. An absolute requirement for oxygen for activity was found. |
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