1983
DOI: 10.1042/bj2110129
|View full text |Cite
|
Sign up to set email alerts
|

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

Abstract: The protein from chicken egg white that inhibits cysteine proteinases, and has been named 'cystatin', was purified by ovomucin precipitation, affinity chromatography on carboxymethylpapain-Sepharose and chromatofocusing. The final purification step separated two major forms of the protein (pI 6.5 and 5.6), with a total recovery of about 20% from egg white. By use of affinity chromatography and immunodiffusion it was shown that the inhibitor is also present at low concentrations in the serum of male and female … Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1
1

Citation Types

3
189
0

Year Published

1989
1989
2015
2015

Publication Types

Select...
7
1

Relationship

0
8

Authors

Journals

citations
Cited by 299 publications
(194 citation statements)
references
References 34 publications
3
189
0
Order By: Relevance
“…Thus, it is quite uncertain as to whether the relative amounts of forms 1 and 2 found after the purification procedures reflect the in vivo situation. Furthermore, since chicken cystatin is not present exclusively in egg white but has also been detected in the serum and in muscle cells [4,24], variable amounts of the two isoelectric forms may be present in different tissues.…”
Section: Discussionmentioning
confidence: 99%
See 2 more Smart Citations
“…Thus, it is quite uncertain as to whether the relative amounts of forms 1 and 2 found after the purification procedures reflect the in vivo situation. Furthermore, since chicken cystatin is not present exclusively in egg white but has also been detected in the serum and in muscle cells [4,24], variable amounts of the two isoelectric forms may be present in different tissues.…”
Section: Discussionmentioning
confidence: 99%
“…By ion-exchange chromatography chicken cystatin can be resolved into two immunologically identical forms with pI values of 6.5 and 5.6 [4], designated as forms A and B [5] or 1 and 2 [4], respectively. The structural differences responsible for the occurrence of two isoelectric forms are a matter of controversy.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…The relative increase in fluorescence was measured at an excitation wavelength of 370 nm and emission wavelength of 460 nm. Inhibition constant, K i , was determined according to the method of Nicklin and Barrett (26) …”
Section: Assay Of Cpi Activitymentioning
confidence: 99%
“…It forms a tight, reversible 1 : 1 complex with most known cysteine proteinases [3]. Chicken egg white cystatin has been reported to occur in two major isoelectric forms, form 1 (pI = 6.5) and form 2 (pl = 5.6), which can be separated by ion exchange chromatography [4,5]. Both forms represent the full-length inhibitors starting with Ser (Ser-form) and comprising 116 amino acid residues Correspondence address: W. Machleidt, Institut ffir Physiologische Chemie, Physikalische Biochemie und Zellbiologie tier Universit~it Miinchen, Goethestrafle 33, D-8000 Miinchen 2, FRG…”
Section: Introductionmentioning
confidence: 99%