Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.26 (invertase)
 4,927 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Endo-N-acetyl-beta-D-glucosaminidase H (Endo H) was purified to homogeneity (3000-fold) from a culture filtrate to Streptomyces plicatus. The key step was substrate-affinity chromatography, which afforded a 1000-fold purification and yielded a protease- and exoglycosidase-free preparation of Endo H. Proteins from the crude sample were applied to the substrate-affinity column, consisting of yeast-invertase glycopeptides bound to Sepharose-immobilized concanavalin A. After washing off the unbound proteins, Endo H was quantitatively eluted by methyl alpha-D-mannopyranoside. Various conditions were tested to achieve an optimal binding of Endo H to this substrate-affinity gel. After substrate-affinity chromatography, Endo H was separated from the coeluted gylcopeptide substrate and some protein impurities by gel filtration and hydrophobic chromatography.
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PMID:Purification of endo-N-acetyl-beta-D-glucosaminidase H by substrate-affinity chromatography. 250 25

Biopsy specimens from 29 adenomas, 17 adenocarcinomas, and 6 synchronous adenomas in cancer patients and from uninvolved mucosa of all main segments of the large bowel were examined histologically and assayed for a series of organelle marker enzymes. Six enzymes--lactase, sucrase, alkaline phosphatase, 5'-nucleotidase, acid phosphatase, and N-acetyl-beta-D-glucosaminidase--showed less activity in adenomas than in adjacent uninvolved mucosa and in specimens from controls. Cancer tissue had higher gamma-glutamyltransferase and lower lactase, alkaline and acid phosphatases, and N-acetyl-beta-D-glucosaminidase activities than specimens from uninvolved mucosa in cancer patients and control patients. Enhanced alkaline phosphatase and N-acetyl-beta-D-glucosaminidase activities were seen in uninvolved mucosa of cancer patients as compared with those of adenoma and control patients. Evidence has been found for multienzyme analysis to identify adenomas with signs of malignant transformation and carcinomas with poor prognosis.
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PMID:Enzyme activities in biopsy specimens from large-bowel mucosa in colorectal adenomas and carcinomas. 362 77

To define reproducible conditions for the homogenization of small-intestinal biopsy samples, tissue homogenization has been studied by the use of three different homogenizers. Tissue samples of increasing wet weights (0.5-10.8 mg) were homogenized in a fixed volume (1 ml) before DNA and protein were determined. The DNA to protein ratio was calculated for all wet weights and used as a measure for reproducible homogenization. The minimum tissue wet weight needed for analysis (2 mg) was determined from the values obtained for the DNA to protein ratio. Highly sensitive techniques are described in detail for the assay of brush border (maltase, lactase, sucrase, neutral alpha-glucosidase, alkaline phosphatase, gamma-glutamyl transferase, leucyl-beta-naphthylamidase), basolateral membrane (5'-nucleotidase), and mitochondrial (succinate dehydrogenase) marker enzymes and for four acid hydrolases (acid phosphatase, acid beta-D-galactosidase, N-acetyl-beta-D-glucosaminidase, acid diesterase) in human and rat jejunal mucosa. Linear kinetics have been established for all enzyme assays. The optimal dilution of tissue homogenate for the assay of the various enzymes has been determined to enable the determination of a maximum number of enzymes in each homogenate. The range of enzyme activities in samples of human and rat jejunal mucosa has been determined.
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PMID:Enzyme activities in human and rat jejunal mucosa. 667 54