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Purification and Properties of a Microsomal Enzyme System Catalyzing the Reactivation of Reduced Ribonuclease and Lysozyme

 Digital Record
Identifier: 101584571X145

Dates

  • Publication: 1964

Extent

5 Pages

Description

In this follow-up to an earlier article, Anfinsen, Goldberger, and Epstein reported "the solubilization and partial purification of the active microsomal protein," and described some of the properties of the soluble system. This and other studies seemed to make clear that the integrity of microsomes as organized particles was not required for catalyzing the reactivation of the reduced forms of ribonuclease and lysozyme. Their findings suggested that the microsomal system might function to facilitate the conversion of at least two different polypeptide chains to the corresponding native proteins during the synthesis of most proteins containing disulfide bonds.

Language of Materials

English

Original Profiles System Identifier

KKBBJY

Source Category

Periodical

Goldberger, Robert, Charles Epstein, and Christian B. Anfinsen. "Purification and Properties of a Microsomal Enzyme System Catalyzing the Reactivation of Reduced Ribonuclease and Lysozyme." Journal of Biological Chemistry 239, 5 (1964): 1406-1410. Article. 5 Images.

Journal of Biological Chemistry

Relation Category

UI (NLM)

KKBBJX

Physical Description

Physical Condition - Good

Photocopy Only

Collecting Area Details

Part of the Archives and Modern Manuscripts Collection Collecting Area

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