The Importance of the Second Hairpin Loop of Cystatin C for Proteinase Binding. Characterization of the Interaction of Trp-106 Variants of the Inhibitor with Cysteine Proteinases-Reference-Cited by-同舟云学术

The Importance of the Second Hairpin Loop of Cystatin C for Proteinase Binding. Characterization of the Interaction of Trp-106 Variants of the Inhibitor with Cysteine Proteinases

Published:1996-01-01 Issue:33 Volume:35 Page:10720-10726
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Björk Ingemar¹,Brieditis Ingrid¹,Raub-Segall Elke¹,Pol Ewa¹,Håkansson Katarina¹,Abrahamson Magnus¹

Affiliation:

1. Department of Veterinary Medical Chemistry, Swedish University of Agricultural Sciences, Uppsala Biomedical Center, Box 575, S-751 23 Uppsala, Sweden, and Department of Clinical Chemistry, University of Lund, University Hospital, S-221 85 Lund, Sweden

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi960420u

Reference33 articles.

1. Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin.

2. Efficient production of native, biologically active human cystatin C byEscherichia coli

3. Human cystatin C. role of the N-terminal segment in the inhibition of human cysteine proteinases and in its inactivation by leucocyte elastase

4. Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum

5. Recombinant chicken egg white cystatin variants of the QLVSG region

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