Ficin and papain inhibitor from chicken egg white

Fossum, Kåre; Whitaker, John R.

doi:10.1016/0003-9861(68)90672-3

Cited by 112 publications

(50 citation statements)

References 31 publications

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“…Cystatin C (CysC) is one of the family of cysteine proteinase inhibitor proteins described for the first time in chick egg white in 1968 (11). Cysteine proteinases (such as the cathepsins B, H and L and the calpains) play a major role in the intracellular catabolism of peptides and proteins through a process of prohormone and proenzyme proteolysis, destruction of collagen and in cancer cells crossing basal membranes.…”

Section: Historymentioning

confidence: 99%

Cystatin C: current position and future prospects

Séronie-Vivien

Delanaye

Piéroni³

et al. 2008

Clinical Chemistry and Laboratory Medicine

163

145

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Cystatin C is a low-molecular-weight protein which has been proposed as a marker of renal function that could replace creatinine. Indeed, the concentration of cystatin C is mainly determined by glomerular filtration and is particularly of interest in clinical settings where the relationship between creatinine production and muscle mass impairs the clinical performance of creatinine. Since the last decade, numerous studies have evaluated its potential use in measuring renal function in various populations. More recently, other potential developments for its clinical use have emerged. This review summarises current knowledge about the physiology of cystatin C and about its use as a renal marker, either alone or in equations developed to estimate the glomerular filtration rate. This paper also reviews recent data about the other applications of cystatin C, particularly in cardiology, oncology and clinical pharmacology. Clin Chem Lab Med 2008;46:1664-86.

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Section: Historymentioning

confidence: 99%

Cystatin C: current position and future prospects

Séronie-Vivien

Delanaye

Piéroni³

et al. 2008

Clinical Chemistry and Laboratory Medicine

163

145

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“…It was originally isolated from egg white [2]; later on two forms of different pI and truncated forms were characterized [3][4][5]. The dissociation constants of their papain complexes were measured ([6] Machleidt, W. et al, submitted).…”

Section: Introductionmentioning

confidence: 99%

Synthesis of a (desSer1 Ile29 Leu89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation

Auerswald¹,

Genenger²,

Assfalg-Machleidt³

et al. 1989

FEBS Letters

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A synthetic gene coding for the cysteine proteinase inhibitor (desSerl Ile29 Leu89) chicken cystatin was cloned and expressed in E. coll. The gene was assembled from 12 oligonucleotides and inserted into vector pUC 8. Expression as fusion protein was performed in a temperature-inducible E. coli system. The expression product was synthesized as 20% of total E. coli protein. The fusion protein was purified, the chicken cystatin homologue was spht off with CNBr and the Nterminal sequence confirmed up to position 37. The properties of the purified material correspond to those of natural chicken cystatin. The recombinant cystatin variant binds anti-chicken cystatin IgG, is inhihitorily active and displays K~ values with papain and with cathepsin B similar to those determined for natural chicken cystatin.

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“…Enzymic digests of calf skin soluble collagen and insoluble tendon collagen were performed at 28°C and at pH values between 3.0 and 6.0 as previously described (Etherington, 1974 Fossum & Whitaker (1968) and fractionated on Sephadex G-75 (superfine grade) as described by Keilova & TomAsek (1974). The effluent fractions were assayed for inhibition of cathepsin Bi and collagenolytic cathepsin.…”

Section: Cross Methodsmentioning

confidence: 99%

Bovine spleen cathepsin B1 and collagenolytic cathepsin. A comparative study of the properties of the two enzymes in the degradation of native collagen

Etherington

1976

Biochemical Journal

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1. Bovine spleen cathepsin Bi and collagenolytic cathepsin were separated by chromatography on Amberlite IRC-50 and collagenolytic cathepsin was partially pOurified by chromatography on DEAE-Sephadex (A-50). 2. Collagenolytic catheps1n degraded insoluble tendon collagen maximally at pH 3.5 and at 28°C; mainly a-chain components were released into solution. At 280C the telopeptides in soluble skin collagen were also cleaved to yield a-chain components. Collagenolytic cathepsin was thus similar to cathepsin Bl in its action against native collagen, but mixtures of these two enzmes exhibited a synergistic effect. 3. The addition of thiol-blocking compounds produced similar inhibition of collagenolytic cathepsin and cathepsin 1B1. The enzymes responded similarly to all other compounds tested except to 6-aminohexanoic acid, when collagenolytic cathepsin was slightly activated and cathepsin Bi was almost unaffected. 4. Leupeptin, which is a structural analogue ofarginine-containing synthetic substrates, inhibited collagenolytic cathepsin as effectively as cathepsin Bi. Collagenolytic cathepsin was shown to retain a low residual activity against c-N-benzoyl-ML-arginine p-nitroanilide during purification which was equivalent to 0.2 % of the activity of cathepsin Bi. 5. Cathepsin 1B1 and collagenolytic cathepsin could not be separated by affinity chromatography on organomercurial-Sepharose 4B. The two enzymnes could be resolved on DEAESephadex (A-50) and by isoelectric-focusing in an Ampholine pH gradient. The pI of the major cathepsin B1 'isoenzyme was 4.9 and the pI of collagenolytic cathepsin was 6.4. 6. From chromatography on Sephadex G-75 (superfine grade) the molecular weights were calculated to be'26000 for cathepsin Bi and 20000 for collagenolytic cathepsin. The difference in molecularweightwasconfirmed by sodium dodecyl sulphate/polyacrylamidegel electrophoresis.

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Ficin and papain inhibitor from chicken egg white

Cited by 112 publications

References 31 publications

Cystatin C: current position and future prospects

Cystatin C: current position and future prospects

Synthesis of a (desSer1 Ile29 Leu89) chicken cystatin gene, expression in E. coli as fusion protein and its isolation

Bovine spleen cathepsin B1 and collagenolytic cathepsin. A comparative study of the properties of the two enzymes in the degradation of native collagen

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