papaya proteinase omega/carica

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Nucleotide sequence and expression in Escherichia coli of cDNAs encoding papaya proteinase omega from Carica papaya.

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Prijava / prijava

We have cloned and sequenced two similar, but distinct, cDNAs from both fruit and leaf tissues of Carica papaya. The C-terminal portion of the predicted amino acid (aa) sequence of one of the clones has complete identity with the mature enzyme sequence of the cysteine proteinase papaya proteinase

The thiol proteinases from the latex of Carica papaya L. IV. Proteolytic specificities of chymopapain and papaya proteinase omega determined by digestion of alpha-globin chains.

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Prijava / prijava

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

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

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

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Prijava / prijava

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

The amino acid sequence of chymopapain from Carica papaya.

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Prijava / prijava

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

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