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| FOLDING INVITRO OF BOVINE PANCREATIC TRYPSIN-INHIBITOR IN THE PRESENCE OF PROTEINS OF THE ENDOPLASMIC-RETICULUM |
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| Author(s): ZAPUN A, CREIGHTON TE, ROWLING PJE, FREEDMAN RB |
| Source: PROTEINS-STRUCTURE FUNCTION AND GENETICS Volume: 14 Issue: 1 Pages: 10-15 Published: SEP 1992 |
| Times Cited: 56 References: 25 |
| Abstract: The rates of folding and disulfide bond formation in reduced BPTI were measured in vitro in the presence and absence of total protein from the endoplasmic reticulum. The rates were increased substantially by the endoplasmic reticulum proteins, but only to the extent expected from the known content and activity of protein-disulfide-isomerase. No effects of added ATP or Ca2+ were observed, even though protein-disulfide-isomerase binds Ca2+ tightly. |
| Document Type: Article |
| Language: English |
Addresses:
1. EUROPEAN MOLEC BIOL LAB, MEYERHOFSTR 1, W-6900 HEIDELBERG, GERMANY
2. UNIV KENT, BIOL LAB, CANTERBURY CT2 7NJ, ENGLAND
3. MRC, MOLEC BIOL LAB, CAMBRIDGE CB2 2QH, ENGLAND |
| Publisher: WILEY-LISS, DIV JOHN WILEY & SONS INC 605 THIRD AVE, NEW YORK, NY 10158-0012 |
| Subject Category: Biochemistry & Molecular Biology; Biophysics |
| IDS Number: JE925 |
| ISSN: 0887-3585 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |