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Purification and Characterization of tripeptidylpeptidase-II From Post-Mortem Human Brain

Purification and Characterization of tripeptidylpeptidase-II From Post-Mortem Human Brain

C Wilson, A M Gibson, J R McDermott

Neurochem Res. 1993 Jul;18(7):743-9.

PMID: 8396212

Abstract:

A soluble tripeptidylaminopeptidase has been isolated from human post-mortem cerebral cortex by anion exchange, hydrophobic interaction and size-exclusion chromatography. From gel filtration studies the active enzyme can exist in both high molecular weight (M(r) > 10(6) and smaller forms. The enzyme hydrolyses Ala-Ala-Phe-7-amido-4-methylcoumarin with a pH optimum of around 7.5 and Km of 148 microM. It did not hydrolyse N-succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin, aminoacyl- or dipeptidyl-7-amido-methylcoumarins and was not inhibited by bestatin. The enzyme was inhibited by phenylmethylsulphonyl-fluoride, 3,4-dichloroisocoumarin, N-hydroxymercuriphenyl-sulphonic acid and N-ethylmaleimide showing that its activity is serine and cysteine dependent. The purified enzyme released tripeptides from several naturally occurring neuropeptides with quite broad specificity. Cholecystokinin octapeptide, angiotensin III and neurokinin A were the most rapidly hydrolysed. Peptides with Pro residues around the point of cleavage were not hydrolysed.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP62037416	Ala-Ala-Phe-7-amido-4-methylcoumarin		62037-41-6	Price
AP71973790	N-Succinyl-Ala-Ala-Phe-7-amido-4-methylcoumarin		71973-79-0	Price

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