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- aggregation classification "A1".
- aggregation creator B41434.
- aggregation creator B41435.
- aggregation creator B41436.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2001".
- aggregation hasFormat 168749.bibtex.
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- aggregation hasFormat 168749.dc.
- aggregation hasFormat 168749.didl.
- aggregation hasFormat 168749.doc.
- aggregation hasFormat 168749.json.
- aggregation hasFormat 168749.mets.
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- aggregation hasFormat 168749.xls.
- aggregation hasFormat 168749.yaml.
- aggregation isPartOf urn:issn:1439-4227.
- aggregation language "eng".
- aggregation subject "Biology and Life Sciences".
- aggregation title "The highly exposed loop region in mammalian purple acid phosphatase controls the catalytic activity.".
- aggregation abstract "Recombinant human purple acid phosphatase (recHPAP) provides a convenient experimental system for assessing the relationship between molecular structure and enzymatic activity in mammalian purple acid phosphatases (PAPs). recHPAP is a monomeric protein with properties similar to those of uteroferrin (Uf) and other PAPs isolated as single polypeptide chains, but its properties differ significantly from those of bovine spleen PAP (BSPAP) and other PAPs isolated as proteolytically "clipped" forms. Incubation of recHPAP with trypsin results in proteolytic cleavage in an exposed region near the active site. The product is a tightly associated two-subunit protein whose collective spectroscopic and kinetics properties resemble those of BSPAP. These results demonstrate that the differences in spectroscopic and kinetics properties previously reported for mammalian PAPs are the result of proteolytic cleavage. Mass spectrometry shows that a three-residue segment, D-V-K, within the loop region is excised by trypsin. This finding suggests that important interactions between residues in the excised loop and one or more of the groups that participate in catalysis are lost or altered upon proteolytic cleavage. Analysis of available structural data indicates that the most important such interaction is that between Asp 146 in the exposed loop and active site residues Asn 91 and His92. Loss of this interaction should result in both an, increase in the Lewis acidity of the Fel ion and an increase in the nucleophilicity of the Fe"'-bound hydroxide ion. Proteolytic cleavage thus constitutes a potential physiological mechanism for regulating the activity of PAP in vivo.".
- aggregation authorList BK104688.
- aggregation endPage "363".
- aggregation issue "5".
- aggregation startPage "355".
- aggregation volume "2".
- aggregation isDescribedBy 168749.
- aggregation similarTo 1439-7633(20010504)2:5355::AID-CBIC3553.0.CO;2-Q.
- aggregation similarTo LU-168749.