Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin
(1992) In Biochemical Journal 281(1). p.49-55- Abstract
- The interaction between recombinant human cystatin C and the cysteine proteinases papain and actinidin was studied by spectroscopic, kinetic and equilibrium methods. The absorption, near-u.v.c.d. and fluorescence-emission difference spectra for the cystatin C-proteinase interactions were all found to be similar to the corresponding spectra for chicken cystatin. The kinetics of binding of cystatin C to the two enzymes were best described by a simple reversible one-step bimolecular mechanism, like the kinetics of the reaction of chicken cystatin with several cysteine proteinases. Moreover, the second-order association rate constants at 25 degrees C, pH 7.4 and I0.15, of 1.1 x 10(7) and 2.4 x 10(6) M-1.s-1 for the reactions of cystatin C with... (More)
- The interaction between recombinant human cystatin C and the cysteine proteinases papain and actinidin was studied by spectroscopic, kinetic and equilibrium methods. The absorption, near-u.v.c.d. and fluorescence-emission difference spectra for the cystatin C-proteinase interactions were all found to be similar to the corresponding spectra for chicken cystatin. The kinetics of binding of cystatin C to the two enzymes were best described by a simple reversible one-step bimolecular mechanism, like the kinetics of the reaction of chicken cystatin with several cysteine proteinases. Moreover, the second-order association rate constants at 25 degrees C, pH 7.4 and I0.15, of 1.1 x 10(7) and 2.4 x 10(6) M-1.s-1 for the reactions of cystatin C with papain and actinidin respectively, were similar to the corresponding rate constants for the chicken inhibitor and close to the value expected for a diffusion-controlled rate. The dissociation equilibrium constants, approx. 11 fM and approx. 19 nM for the binding of cystatin C to papain and actinidin respectively, were also comparable with the dissociation constants for chicken cystatin. The affinity between cystatin C and several inactivated papains or actinidins decreased with increasing size of the inactivating group in a manner similar to that in earlier studies with the chicken inhibitor. Together, these results strongly indicate that the mechanisms of the reactions of cystatin C and chicken cystatin with cysteine proteinases are identical or highly similar, but differ from that of reactions between serine-proteinase inhibitors and their target enzymes. The model for the proteinase-inhibitor interaction, based on the X-ray structure of chicken cystatin, therefore should be largely applicable also to human cystatin C. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1106372
- author
- Lindahl, P ; Abrahamson, Magnus LU and Björk, I
- organization
- publishing date
- 1992
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biochemical Journal
- volume
- 281
- issue
- 1
- pages
- 49 - 55
- publisher
- Portland Press
- external identifiers
-
- pmid:1731767
- scopus:0026570448
- ISSN
- 0264-6021
- language
- English
- LU publication?
- yes
- id
- 4070a525-79a1-414d-aecd-416ee3238f05 (old id 1106372)
- alternative location
- http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1130639&blobtype=pdf
- date added to LUP
- 2016-04-01 16:36:38
- date last changed
- 2021-01-31 03:39:18
@article{4070a525-79a1-414d-aecd-416ee3238f05,
abstract = {{The interaction between recombinant human cystatin C and the cysteine proteinases papain and actinidin was studied by spectroscopic, kinetic and equilibrium methods. The absorption, near-u.v.c.d. and fluorescence-emission difference spectra for the cystatin C-proteinase interactions were all found to be similar to the corresponding spectra for chicken cystatin. The kinetics of binding of cystatin C to the two enzymes were best described by a simple reversible one-step bimolecular mechanism, like the kinetics of the reaction of chicken cystatin with several cysteine proteinases. Moreover, the second-order association rate constants at 25 degrees C, pH 7.4 and I0.15, of 1.1 x 10(7) and 2.4 x 10(6) M-1.s-1 for the reactions of cystatin C with papain and actinidin respectively, were similar to the corresponding rate constants for the chicken inhibitor and close to the value expected for a diffusion-controlled rate. The dissociation equilibrium constants, approx. 11 fM and approx. 19 nM for the binding of cystatin C to papain and actinidin respectively, were also comparable with the dissociation constants for chicken cystatin. The affinity between cystatin C and several inactivated papains or actinidins decreased with increasing size of the inactivating group in a manner similar to that in earlier studies with the chicken inhibitor. Together, these results strongly indicate that the mechanisms of the reactions of cystatin C and chicken cystatin with cysteine proteinases are identical or highly similar, but differ from that of reactions between serine-proteinase inhibitors and their target enzymes. The model for the proteinase-inhibitor interaction, based on the X-ray structure of chicken cystatin, therefore should be largely applicable also to human cystatin C.}},
author = {{Lindahl, P and Abrahamson, Magnus and Björk, I}},
issn = {{0264-6021}},
language = {{eng}},
number = {{1}},
pages = {{49--55}},
publisher = {{Portland Press}},
series = {{Biochemical Journal}},
title = {{Interaction of recombinant human cystatin C with the cysteine proteinases papain and actinidin}},
url = {{http://www.pubmedcentral.nih.gov/picrender.fcgi?artid=1130639&blobtype=pdf}},
volume = {{281}},
year = {{1992}},
}