Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.5.1.52 (PNGase F)
 1,527 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Aldosterone induces the synthesis of a group of glycoproteins (GP65,70) in toad urinary bladders which are potential effectors of the natriferic action of this hormone. The GP65,70 complex is composed of two molecular weight classes of proteins (Mr 65 and 70 kDa), each class being composed of several discrete proteins of varying isoelectric points (5.8-6.2). These proteins can be partially enriched (approximately 20-fold) using wheat germ agglutinin-sepharose affinity chromatography, are neuraminidase-resistant, and can be N-deglycosylated by endoglycosidase-H and N-glycanase. Treatment with N-glycanase leads to the appearance of a microheterogeneous group of proteins, all having the same Mr (approximately 40 kDa). From these studies it can be concluded that these particular aldosterone-induced proteins: (1) are heavily glycosylated, (2) contain multiple high mannose and hybrid oligosaccharides side chains, and (3) contain similar (if not identical) peptide backbones. Post-translational N-glycosylation accounts, at least in part, for their electrophoretic polymorphism (variation in Mr) but not for their electrophoretic microheterogeneity (variation in pI). The latter may reflect other types of post-translational modification (e.g. O-glycosylation, phosphorylation) or may be due to subtle differences in amino acid composition. The partial purification and biochemical characterization of GP65,70 should ultimately lead to a better understanding of the function of these putative "effectors" of aldosterone-stimulated Na+ transport.
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PMID:Aldosterone-induced glycoproteins: further characterization. 250 87

The major coagulating fibrinogenase of Deinagkistrdon acutus venom, designated acutobin, was purified by anion-exchange chromatography, gel filtration and reverse-phase HPLC. Approximately 80% of its protein sequence was determined by sequencing the various fragments derived from CNBr cleavage and digestion with endoprotease. Extensive screening of the venom gland cDNA species after amplification by PCR resulted in the isolation of four distinct cDNA clones encoding acutobin and three other serine proteases, designated Dav-PA, Dav-KN and Dav-X. The complete amino acid sequences of these enzymes were deduced from the cDNA sequences. The amino-acid sequence of acutobin contains a single chain of 236 residues including four potential N-glycosylation sites. The purified acutobin (40 kDa) contains approx. 30% carbohydrate by weight, which could be partly removed by N-glycanase. The phylogenetic tree of the complete amino acid sequences of 40 serine proteases from 18 species of Crotalinae shows functional clusters reflecting parallel evolution of the three major venom enzyme subtypes: coagulating enzymes, kininogenases and plasminogen activators. The possible structural elements responsible for the functional specificity of each subtype are discussed.
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PMID:Serine protease isoforms of Deinagkistrodon acutus venom: cloning, sequencing and phylogenetic analysis. 1117 Oct 91