Immunochemical studies of human erythrocyte proteins: erythrocuprein and catalase.

نویسندگان

  • M J Stansell
  • H F Deutsch
چکیده

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 erythrocyte catalase is not immunochemically identical with human liver catalase. Rabbit antisera to erythrocyte catalase fail to precipitate with hemolysates from some higher primates but give a cross-reaction with lysates from the cat and pig. Human erythrocuprein antisera give a cross-reaction only with hemolysate from the higher primates.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

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...

متن کامل

Preparation of Crystalline Erythocuprein 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...

متن کامل

A modified method for the purification of erythrocuprein.

A copper-containing protein named haemocuprein was isolated from the erythrocytes of different mammals by MANN AND KEILIN 1. The preparation from ox-blood contained 0.34 % Cu, and there was evidence that the protein was obtained in a highly purified state. The authors also tried to purify a corresponding protein from human erythrocytes and obtained a preparation with a copper content of o.21%, ...

متن کامل

Isolation of human hepatocuprein and cerebrocuprein. Their identity with erythrocuprein.

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...

متن کامل

Methaemoglobin Content and NADH-Methaemoglobin Reductase Activity of Three Human Erythrocyte Genotypes

Background: To study methaemoglobin content and NADH-methaemoglobin reductase activity of three human erythrocyte genotypes (HbAA, HbAS and HbSS).Materials and Methods: Studies to ascertain methaemoglobin concentration and level of NADH-methaemoglobin reductase activity of three human erythrocyte genotypes (HbAA, HbAS and HbSS) were carried out in forty-three (43) healthy male participants of c...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • The Journal of biological chemistry

دوره 241 11  شماره 

صفحات  -

تاریخ انتشار 1966