Chymopapain C, an Immunosuppressive Protease: I. Partial Purification and Characterization

Clagett, James; Tokuda, Sei; Engelhard, Warren E.

doi:10.3181/00379727-145-37991

Cited by 12 publications

(5 citation statements)

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“…Fluorescein isothiocyanate (FITC) labeled goat anti-human Fab antiserum was the gift of Dr. lames Clagett and was found to be free of antibody to the test organisms. It was prepared by repeated injection of an adult goat with Fab fragments from chymopapain C-digested normal human IgG (Clagett, Tokuda and Engelhard, 1974). The isolated goat IgG was fluorochrome labeled by the method of Clark and Shepard (1963).…”

Section: Immunological Proceduresmentioning

confidence: 99%

Subgingival microflora and periodontitis

Williams

Pantalone

Sherris

1976

J of Periodontal Research

147

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Predominant bacterial flora resident in subgingival plaque was characterized and evaluated in relation to the etiology of periodontal disease. Small groups of clinically and radiographically identified periodontal patients and control subjects were studied. A comprehensive inventory of cultivable flora was made. The most common group of organisms were the Gram‐positive rods, the majority of which were Actinomyces. A larger proportion of anaerobic Gram‐negative rods were isolated than indicated in the results of previous studies. Considerable variability in floral content was found in different sites in the same patient. However, no statistically significant differences were observed in the flora between clinically normal and pathological sites of the same patients. A significantly greater number of facultative Actinomyces was present in the flora of periodontal patients as compared to control subjects. Sera from the same nine subjects were assayed by indirect immunofluorescence for circulating antibodies to 12 strains of plaque bacteria. No differences in antibody titers were observed between sera from periodontal patients and control subjects.

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Section: Immunological Proceduresmentioning

confidence: 99%

Subgingival microflora and periodontitis

Williams

Pantalone

Sherris

1976

J of Periodontal Research

147

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“…Each of these enzymes can occur in immunologically identical multiple forms differing in molecular charge; these are particularly marked for chymopapain (Kunimitsu & Yasunobu, 1967;Buttle & Barrett, 1984). There have been preliminary reports suggesting the presence of other cysteine proteinases in papaya latex (Schack, 1967;Clagett et al, 1974;Lynn, 1979). To date these have not been followed up.…”

Section: Introductionmentioning

confidence: 99%

Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex

Buttle¹,

Kembhavi²,

Sharp³

et al. 1989

Biochemical Journal

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A procedure is described for the purification of a previously undetected cysteine proteinase, which we have called papaya proteinase IV, from spray-dried latex of the papaya (Carica papaya) plant. The purification involves affinity chromatography on Gly-Phe-aminoacetonitrile linked to CH-Sepharose 4B, with elution by 2-hydroxyethyl disulphide at pH 4.5. The product thus obtained is a mixture of almost fully active papain and papay proteinase IV, which are then separated by cation-exchange chromatography. A preliminary characterization of papaya proteinase IV showed it to be very similar to chymopapain in both molecular size and charge. However, the new enzyme is immunologically distinct from the previously characterized cysteine proteinases of papaya latex. It also differs in its lack of activity against the synthetic substrates of the other papaya proteinases, in its narrow specificity against protein substrates and its lack of inhibition by chicken cystatin. Papaya proteinase IV is abundant, contributing almost 30% of the protein in spray-dried papaya latex, and contamination of chymopapain preparations with this enzyme may account for some of the previously reported heterogeneity of chymopapain.

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“…It has recently achieved medical importance through its use in the treatment of prolapsed intervertebral discs (Javid et al, 1983). Chymopapain purified from spray-dried latex is well known to be heterogeneous on cation-exchange chromatography (Baines & Brocklehurst, 1982;Clagett et al, 1974;Khan & Polgar, 1983;Kunimitsu & Yasunobu, 1967;Lynn, 1979;Robinson, 1975;Schack, 1967). Normally, the material eluted early from the cation-exchange column is called 'chymopapain A' and is followed by an incompletely resolved peak of 'chymopapain B'.…”

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confidence: 99%

Chymopapain. Chromatographic purification and immunological characterization

Buttle¹,

Barrett²

1984

Biochemical Journal

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Chymopapain (EC 3.4.22.6) was purified from commercially available spray-dried latex of papaya (Carica papaya) fruit by (NH4)2SO4 fractionation and fast protein chromatography on the Mono S cation-exchange column. Multiple forms of chymopapain separated chromatographically were shown to be immunologically identical. A major form was isolated and found to be homogeneous by several criteria, and fully active, and its N-terminal amino acid was identified as tyrosine. Latex from fresh unripe papaya fruit contained predominantly one form of chymopapain, and it is concluded that chymopapain is a single enzyme distinct from the other cysteine proteinases of C. papaya latex.

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Chymopapain C, an Immunosuppressive Protease: I. Partial Purification and Characterization

Cited by 12 publications

References 0 publications

Subgingival microflora and periodontitis

Subgingival microflora and periodontitis

Affinity purification of the novel cysteine proteinase papaya proteinase IV, and papain from papaya latex

Chymopapain. Chromatographic purification and immunological characterization

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