Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P00790 (PGA)
 2,475 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have shown that thrombospondin (tsp), like fibronectin (fn) and von Willebrand factor (vWf), exhibits a rapid, specific and saturable binding to collagen type I fibres (from bovine tendon). The level of binding at saturation is very similar to that of vWf. As with fn and vWf, the interaction is ionic in character and appears to occur by a polyvalent mechanism since there is little inhibition of interaction by monomeric collagen. The conformation of tsp, like that of fn and vWf, is important since denaturation causes reduced complexing. Furthermore, conformational changes in tsp due to the presence of Ca++ can modulate the amount of complex formed under physiological conditions. Tsp, like vWf but in contrast to fn, shows little affinity for denatured fibres emphasizing the importance of collagen conformation. Pepsin digestion suggests an important role for collagen telopeptides; vWf- and fn-binding sites are located more within the collagen triple helix. Comparison of the effect on binding after leucine aminopeptidase or carboxypeptidase digestion suggests involvement of the N- rather than C-terminal telopeptides. No evidence was found for a role for fn, the proteoglycan PG2 or collagen type V, which could be present in type I fibres, in mediating the interaction between tsp and the fibres. VWf did not inhibit the interaction of tsp, but fn did slightly when tested in large excess. This suggests separate binding sites in collagen for all three ligands since fn and vWf are also known to bind independently of each other.
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PMID:Characterization of thrombospondin binding to collagen (type I) fibres: role of collagen telopeptides. 187 Apr 47

Two extracellular isoenzymes of polygalacturonases PG1 and PG2 were isolated from 3-day-old culture filtrates of Trichoderma reesei. The two enzymes were purified to homogeneity by ion-exchange, gel filtration and hydrophobic interaction chromatographies. PG1 and PG2 exhibit similar molecular weights from gel filtration and SDS-PAGE. Their properties, including optimal pH and temperature, thermal stability and Km were compared. Characterization of substrate specificity showed that the two enzymes had higher affinity toward PGA (B0100) derived from sugar beet pectin (SBP) than PGA from lime pectin. A series of SBPs with different distribution patterns of methyl and acetyl groups, produced by treatment with either plant pectin methylesterase (P-series) or fungal pectin methylesterase (F-series) or base catalysis (B-series), was used as substrates for PG1 and PG2. Substrates with a low degree of esterification were preferred substrates. The activities of PG1 and PG2 were strongly correlated to the degree of methylation and very little effect from acetylation. The products generated by digestion of selected lime and SBPs were analysed using matrix assisted laser desorption ionisation time of flight (MALDI TOF) MS. A mode of action revealed a random cleavage pattern for PG1 and PG2, confirming that these enzymes are endopolygalacturonases.
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PMID:New polygalacturonases from Trichoderma reesei: characterization and their specificities to partially methylated and acetylated pectins. 1266 7