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chymopapain/melonenbäume

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The thiol proteinases from the latex of Carica papaya L. III. The primary structure of chymopapain.

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The amino-acid sequence of chymopapain is presented. It was isolated from the latex of the fruits from the tropical species Carica papaya L. and is, besides papain and papaya proteinase omega, the third thiol proteinase from this source. The primary structure contains 218 amino-acid residues. It was

Separation of chymopapain from papaya latex (Carica papaya) on amberlite IR-120 (Hg2+).

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The quantitative separation of chymopapain from papaya latex has been carried out by chromatography on Amberlite IR-120 (Hg2+). The product obtained was further studied to determine its homogeneity.
The proteolytic specificities of chymopapain and papaya proteinase omega were investigated by using the alpha-chains of manatee and mole haemoglobin, whose primary structures are known, as substrates. The resulting peptides from each enzymatic cleavage were isolated by gel filtration on Sephadex

The amino acid sequence of chymopapain from Carica papaya.

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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

Fresh non-fruit latex of Carica papaya contains papain, multiple forms of chymopapain A and papaya proteinase omega.

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Isolation and preliminary characterization of the cysteine-proteinases from the latex of Carica candamarcensis Hook.

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The cysteine-proteinase chymopapain from Carica papaya L. is used for chemonucleolysis of damaged human intervertebral spinal discs. The purification of this enzyme is difficult. To overcome these problems, we were looking for a substitute among the cysteine-proteinases of Carica candamarcensis

Primary structure of CC-III, the glycosylated cysteine proteinase from the latex of Carica candamarcensis Hook.

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The amino acid sequence of the cysteine proteinase CC-III from the latex of the subtropical species Carica candamarcensis Hook has been determined with the exception of seven residues (pos. 180-186). It was deduced from the sequence analysis of the whole chain and peptides obtained by tryptic,

Factors effecting the thermostability of cysteine proteinases from Carica papaya.

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Thermal denaturation of four Carica papaya cysteine proteinases (papain, chymopapain, papaya proteinases 3 and 4) was studied as a function of pH using high-sensitivity differential scanning calorimetry. The ratios of calorimetric enthalpy to Van't Hoff enthalpy suggest that, for all these proteins,

The structure of CMS2MS2, a mitogenic protein isolated from Carica candamarcensis.

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In a recent study we showed that two proteinases (CMS2MS2 and CMS2MS3) from Carica candamarcensis enhance mammalian cell proliferation. The aim of the present study is the determination of the primary structure of CMS2MS2 and prediction of its three-dimensional structure. The protein contains 214

Effects of mechanical wounding on Carica papaya cysteine endopeptidases accumulation and activity.

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The mechanical wounding impact on the Carica papaya latex protein pattern was investigated by analyzing three latexes. A first one commercially available, a second harvested from unripe but fully grown fruits, both obtained from regularly tapped fruits. A third one was collected from similar fruits

Molecular cloning of two cysteine proteinases from paw-paw (Carica papaya).

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Two cDNA clones for plant cysteine proteinases have been isolated from a Carica papaya (paw-paw, papaya) leaf tissue cDNA library by using a mixture of 16 synthetic oligodeoxyribonucleotides as a hybridization probe. The inserted regions are 311 and 440 base-pairs in length and have the potential to

The thiol proteinases from the latex of Carica papaya L. I. Fractionation, purification and preliminary characterization.

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Three thiol proteinases, namely papain, chymopapain and proteinase omega were purified to homogeneity from the latex of Carica papaya L. During the purification procedure, the thiol function of the cysteinyl residues were protected either as mixed disulfides with cysteamine or 2-thiopyridone or as
In the tropical species Carica papaya, the articulated and anastomosing laticifers form a dense network of vessels displayed in all aerial parts of the plant. Damaging the papaya tree inevitably severs its laticifers, eliciting an abrupt release of latex. Besides the well-known cysteine proteinases,
Papaya meleira virus (PMeV) is so far the only described laticifer-infecting virus, the causal agent of papaya (Carica papaya L.) sticky disease. The effects of PMeV on the laticifers' regulatory network were addressed here through the proteomic analysis of papaya latex. Using both 1-DE- and

Fractionation and purification of the enzymes stored in the latex of Carica papaya.

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The latex of the tropical species Carica papaya is well known for being a rich source of the four cysteine endopeptidases papain, chymopapain, glycyl endopeptidase and caricain. Altogether, these enzymes are present in the laticifers at a concentration higher than 1 mM. The proteinases are
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