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Journal article

The conformation of calreticulin is influenced by the endoplasmic reticulum luminal environment.

Abstract:

In order to understand the dynamics of the endoplasmic reticulum (ER) luminal environment, we investigated the role of Ca(2+), Zn(2+), and ATP on conformational changes of calreticulin. Purified calreticulin was digested with trypsin in the presence or absence of Ca(2+), Zn(2+), and ATP. At low Ca(2+) concentration (<100 micrometer), calreticulin is rapidly and fully degraded by trypsin, indicating that under these conditions the protein is in a highly trypsin-susceptible conformation. Inc...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.M002049200

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Journal:
Journal of biological chemistry More from this journal
Volume:
275
Issue:
35
Pages:
27177-27185
Publication date:
2000-09-01
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
Language:
English
Keywords:
Pubs id:
pubs:156305
UUID:
uuid:24d027eb-7024-4e19-b08a-50276e748139
Local pid:
pubs:156305
Source identifiers:
156305
Deposit date:
2012-12-19

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