Physicochemical Studies of Crystalline Human Erythrocuprein
نویسندگان
چکیده
منابع مشابه
Preparation of crystalline erythrocuprein and catalase from human erythrocytes.
The removal of hemoglobin from blood cell lysates used for the preparation of various erythrocyte enzymes has been commonly achieved by denaturation through the use of a chloroform-ethanol mixture, the so-called Tsuchihashi procedure (1). Although there has been speculation concerning possible modification of the nonhemoglobin protein by such treatment (2, 3), no clear cut, alternative, large s...
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The immunochemical properties of chromatographically prepared human erythrocuprein differ from those of the chloroform-ethanol-treated protein. Losses of copper also appear to modify its immunochemical reactivity. The result of the immunochemical reactions of rabbit antibody to human erythrocuprein with human liver and brain extracts suggests a common antigen in the two tissues. Human erythrocy...
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Plasminogen (profibrinolysin) of high specific activity has been prepared from human sources and converted to plasmin (fibrinolysin) by a variety of means (3, 4). Since these preparations seemed to possess activities of as high an order as any that had yet been produced, it was considered appropriate to examine their purity by physicochemical means. Such investigations do not appear to have bee...
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Cerebrocuprein and hepatocuprein have been isolated from extracts of human brain and liver, respectively, by a method which utilizes ion exchange chromatography and gel filtration procedures. Detailed studies of the physical, chemical, and immunological properties of the purified proteins were conducted. A comparison of the results with similar data obtained for erythrocuprein from human erythr...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1965
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)97060-2