scispace - formally typeset
J

J P G Malthouse

Researcher at University College Dublin

Publications -  57
Citations -  1242

J P G Malthouse is an academic researcher from University College Dublin. The author has contributed to research in topics: Oxyanion & Subtilisin. The author has an hindex of 20, co-authored 57 publications receiving 1205 citations. Previous affiliations of J P G Malthouse include Texas A&M University & St Bartholomew's Hospital.

Papers
More filters
Journal ArticleDOI

A reporter group delivery system with both absolute and selective specificity for thiol groups and an improved fluorescent probe containing the 7-nitrobenzo-2-oxa-1,3-diazole moiety

TL;DR: Spectral analysis of the reactions of compound (I) with L-cysteine and with papain showed that even under equimolar conditions the reaction is essentially stoicheimoetric and probably proceeds by specific attack at the sulphur atom distal from the pyridyl ring of compounds (I).
Journal ArticleDOI

13C NMR analysis reveals a link between L-glutamine metabolism, D-glucose metabolism and γ-glutamyl cycle activity in a clonal pancreatic beta-cell line

TL;DR: It is proposed that L-glutamine metabolism is important in the beta cell for generation of stimulus-secretion coupling factors, precursors of glutathione synthesis and for supplying carbon for oxidation in the TCA cycle.
Journal ArticleDOI

Differences in the interaction of the catalytic groups of the active centres of actinidin and papain Rapid purification of fully active actinidin by covalent chromatography and characterization of its active centre by use of two-protonic-state reactivity probes

TL;DR: Actinidin was shown to resemble ficin rather than papain in (i) the disposition of the active-centre imidazole group with respect to hydrophobic binding areas, and (ii) the inability of the Active Centre aspartic acid carboxy group to influence the reactivity of theActive Centre thiol group at pH values of about 4.4.
Journal ArticleDOI

Studying enzyme mechanism by 13C nuclear magnetic resonance.

TL;DR: The proteases trypsin and papain are shown to form tetrahedrally coordinated complexes and acyl derivatives with a variety of compounds artificially enriched at the site or sites of interest.