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Carboxypeptidase N from pig serum
Hoppe-Seyler'S Zeitschrift Fur Physiologische Chemie
|June 1, 1976
Summary
Carboxypeptidase N, purified from pig serum, has a molecular weight of 315,000 and dissociates into three subunits. Trypsin treatment enhances its activity and reduces its molecular weight.
Area of Science:
- Biochemistry
- Enzymology
Background:
- Carboxypeptidase N is a key enzyme involved in protein metabolism.
- Understanding its structure and function is crucial for various biological processes.
Purpose of the Study:
- To purify and characterize Carboxypeptidase N from pig serum.
- To investigate the enzyme's subunit composition and the effect of trypsin on its activity.
Main Methods:
- Purification of Carboxypeptidase N from pig serum using established biochemical techniques.
- Determination of molecular weight and subunit composition via SDS-PAGE.
- Analysis of carbohydrate content in native enzyme and subunits.
- Enzymatic assays to assess the effect of trypsin treatment.
Main Results:
- Carboxypeptidase N was purified 865-fold with a native molecular weight of approximately 315,000.
- The enzyme comprises three subunits (90,000, 50,000, and 30,000 Da).
- The 90,000 Da subunit contains carbohydrate, while the other two do not.
- Trypsin treatment resulted in a lower molecular weight and increased enzyme activity.
Conclusions:
- Carboxypeptidase N is a multi-subunit glycoprotein.
- Enzymatic modification by trypsin alters its molecular weight and enhances its catalytic activity.
- These findings contribute to the understanding of Carboxypeptidase N's structure-function relationship.