The amino acid sequence of chymopapain from Carica papaya

Abstract

Chymopapain is a polypeptide of 218 amino acid residues. It has considerable structural similarity with papain and papaya proteinase omega, including conservation of the catalytic site and of the disulphide bonding. Chymopapain is like papaya proteinase omega in carrying four extra residues between papain positions 168 and 169, but differs from both papaya proteinases in the composition of its S2 subsite, as well as in having a second thiol group, Cys-117. Some evidence for the amino acid sequence of chymopapain has been deposited as Supplementary Publication SUP 50153 (12 pages) at the British Library Document Supply Centre, Boston Spa., Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies may be obtained on the terms indicated in Biochem. J. (1990) 265, 5. The information comprises Supplement Tables 1-4, which contain, in order, amino acid compositions of peptides from tryptic, peptic, CNBr and mild acid cleavages, Supplement Fig. 1, showing re-fractionation of selected peaks from Fig. 2 of the main paper. Supplement Fig. 2, showing cation-exchange chromatography of the earliest-eluted peak of Fig. 3 of the main paper, Supplement Fig. 3, showing reverse-phase h.p.l.c. of the later-eluted peak from Fig. 3 of the main paper, and Supplement Fig. 4, showing the separation of peptides after mild acid hydrolysis of CNBr-cleavage fragment CB3.

Amino‐acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale

“…For this reason, and because of the ambiguities discussed above, the GP-I sequence reported here must be regarded as tentative. The appearance of multiple forms of the ginger proteases is not remarkable, however, as such heterogeneity has also been seen in other species, for example, papaya [24] and pineapple stem [25]. The N-linked oligosaccharides of plant glycoproteins typically have 5±13 glycosyl units and fall into two main classes: high-mannose-type glycans and complex-type glycans.…”

Purification of a Cysteine Proteinase from Carica candamarcensis L. and Cloning of a Genomic Putative Fragment Coding for This Enzyme

“…The highest concentration of profile of CC23 obtained after Mono S chromatography. Samples (1)(2)(3)(4)(5) inhibitor shown represents the minimum amount required to attain g) were boiled 5 min in sample buffer containing 2.5 MS and applied maximal inhibition. onto SDS-PAGE.…”

Low versus high molecular weight poly(ethylene glycol)‐induced states of stem bromelain at low pH: Stabilization of molten globule and unfolded states

“…[4][5][6] Recent evidence, however, supports the idea that MG may also possess well-defined tertiary contacts. [7][8][9] The stem bromelain (SB), from Ananas cosmosus, like other cysteine proteinases, belongs to the þ protein class, and the highly similar amino acid sequences of papain, 10 actinidin, 11 proteinase O, 12 chymopapain, 13 and SB 14 indicate that the polypeptide chains of these proteins may share a common folding pattern. This has been substantiated for the former three proteinases by detailed X-ray diffraction studies.…”