Studies of the copper transfer between native laccase and apostellacyanin

Studies of the copper transfer between native laccase and apostellacyanin

188 Abstracts STUDIES OF THE COPPER TRANSFER BETWEEN NATIVE UCCASE AND APOSTELLACYANIN. Kellev A. Burns and David R. McMillin, Purdue University, West...

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188 Abstracts STUDIES OF THE COPPER TRANSFER BETWEEN NATIVE UCCASE AND APOSTELLACYANIN. Kellev A. Burns and David R. McMillin, Purdue University, West Lafayette, IN 47907-3699, USA.

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Lactase, a multi-copper oxidase, was studied as a copper transfer agent, using apostellacyanin as a copper recipient. Lactase was studied in this regard to provide some insight into its function as a possible copper transport agent in the lacquer tree and to serve as a model of ceruloplasmin. Under reducing conditions, it was found that lactase partially reconstituted apostellacyanin, thus indicating that it could indeed function as a copper transport agent, in vitro. Only about 15% of the total copper in lactase could be transferred. Studies were conducted to provide insight into possible site specificity of copper loss from lactase.

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A STUDY OF MO-PROTEINS AND GENES RELEVANT TO MO TRANSPORT AND METABOLISM IN ESCHERICHIA COLI S. M. Hinton, M. Grossman, and V. Minak-Bernero, Exxon Researchand Engineering Co., Rt. 22 East, Annandale, NJ 08801, USA. We have identified the MO-binding proteins and the chl gene products in &. coli in order to understand their relationship in Mo-cofactor biosynthesis. The Chl proteins are required for MO-binding to protein, efficient utilization of MO, maturation of Mo-cofactor, and active transport of MO. Genetic and biochemical studies have revealed a MO transport operon, and two MO-binding transport proteins. Promoter-h fusions have been used to study the factors regulating the operon.

PURIFICATION OF A PROTEIN ASSOCIATED WITH ZN REDISTRIBUTION IN D014 CITRUS . K. C. Taylor-l, L. G. Albrigo2, C. D. Chasel. Vegetable Crops Dept., Univ. of Florida, Gainesville, FL 32611. 2Citrus Res. and Ed. Center, Univ. of Florida, Lake Alfred, FL 33850. A 4.5 kd Zn-binding protein present in healthy citrus phloem tissue was isolated at increased quantity from phloem of blight-affectedcitrus. Citrus blight is a decline of unknown etiology, with Zn redistribution from leaves to phloem as the earliest observed symptom. The protein appears to be of plant origin since it occurs in healthy citrus phloem tissue. The protein, purified to homogeneity, has an amino acid composition which indicates it is a direct gene product. Characterization of the protein and its metal-binding properties is underway and will be reported. Supported by USDA Competitive Res. Grant #86-CRCR-l-2081.