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Dipeptidyl peptidase III is a zinc metallo-exopeptidase. Molecular cloning and expression.
We have purified dipeptidyl peptidase III (EC 3.4.14.4) from human placenta. It had a pH optimum of 8.8 and readily hydrolysed Arg-Arg-beta-naphthylamide. Monoamino acid-, Gly-Phe-, Gly-Pro- andExpand
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Aspartic acid 405 contributes to the substrate specificity of aminopeptidase B.
Aminopeptidase B (EC 3.4.11.6, ApB) specifically cleaves in vitro the N-terminal Arg or Lys residue from peptides and synthetic derivatives. Ap B was shown to have a consensus sequence found in theExpand
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The HELLGH motif of rat liver dipeptidyl peptidase III is involved in zinc coordination and the catalytic activity of the enzyme.
The role of the HELLGH (residues 450-455) motif in the sequence of rat dipeptidyl peptidase III (EC 3.4.14.4) was investigated by replacing Glu451 with an alanine or an aspartic acid residue and byExpand
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Purification and properties of dipeptidyl peptidase IV from Streptococcus mitis ATCC 9811.
Abstract Dipeptidyl peptidase IV (EC 3.4.14.—) from Streptococcus mitis ATCC 9811 was purified to a specific activity of 56.2 units/mg protein by a series of column chromatographic techniques. TheExpand
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Inorganic Pyrophosphatase Activity of Purified Bovine Pulp Alkaline Phosphatase at Physiological pH
At physiological pH, the hydrolytic activity of purified bovine pulp alkaline phosphatase toward phosphorus compounds was observed to be in the order of inorganic pyrophosphate > β-glycerophosphate >Expand
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Metal Preferences of Zinc-Binding Motif on Metalloproteases
Almost all naturally occurring metalloproteases are monozinc enzymes. The zinc in any number of zinc metalloproteases has been substituted by some other divalent cation. Almost all Co(II)- orExpand
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  • Open Access
Purification and properties of dipeptidyl peptidase II from rat kidney.
Dipeptidyl peptidase II (EC 3.4.14.2) from rat kidney was purified to a specific activity of 66.2 mumol/min per mg protein by a series of column chromatographic techniques. The purified enzyme wasExpand
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Inhibitory action of proline-containing peptides on Xaa-Pro-dipeptidylaminopeptidase.
Abstract The inhibitory action of proline-containing peptides such as Gly-Pro, Gly-Pro-Hyp, Pro-Gly, Pro-Gly-Gly, Pro-Pro and Pro-Pro-Pro-Pro ((PrO)4) on Xaa-Pro-dipeptidylaminopeptidase from pigExpand
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Molecular Cloning and Expression of Rat Liver Aminopeptidase B*
We isolated, by immunological screening of a Uni-ZAP XR cDNA library constructed from rat liver mRNAs, a cDNA clone with 2212 base pairs encoding aminopeptidase B (EC 3.4.11.6). The open readingExpand
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Purification, partial sequencing and characterization of an insect membrane dipeptidyl aminopeptidase that degrades the insect neuropeptide proctolin.
Two proctolin-binding proteins solubilized from 1600 cockroach hindgut membranes were purified 1000-fold using five chromatography steps. Twenty-five micrograms of protein were recovered from theExpand
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