958. The preparation and properties of acetochloroglucosamine and its use in the synthesis of 2-acetamido-2-deoxy-β-<scp>D</scp>-glucosides (N-acetyl-β-<scp>D</scp>-glucosaminides)

Leaback, David H.; Walker, P. G.

doi:10.1039/jr9570004754

Cited by 69 publications

(18 citation statements)

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“…Preparation of Substrates.-Phenyl, p-nitrophenyl, and ac-naphthyl N-acetyl-p-D-glucosaminides were prepared by the method of Leaback and Walker (1957). Estimation of N-Acetyl-3-glucosaminidase in Serum.-The absorption of p-nitrophenyl liberated by N-acetyl-3-glucosaminidase from p-nitrophenyl N-acetyl-p-glucosamide was estimated in alkaline solution at 400 msu in a " unicam " SP 500 spectrophotometer. The absorption of unhydrolysed substrate at this wavelength is negligible.…”

Section: Methodsmentioning

confidence: 99%

N-Acetyl-Β-Glucosaminidase ACTIVITY IN SERUM DURING PREGNANCY

1960

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A spectrophotometric method for the estimation of N-acetyl-,B-glucosaminidase in serum has been devised. Sera from normal adult males and females showed similar levels of activity.The activity in serum rose progressively during pregnancy and fell rapidly after parturition to normal levels. This change resembled closely that which occurs in serum ,B-glucuronidase.Placenta showed a moderate and chorion a high level of N-acetyl-,-glucosaminidase. High N-acetyl-p-glucosaminidase activity was demonstrated histochemically in decidual cells.

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Section: Methodsmentioning

confidence: 99%

N-Acetyl-Β-Glucosaminidase ACTIVITY IN SERUM DURING PREGNANCY

1960

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“…N*AcOyI-f4n-hexosao8iidWase (EC 3.ZI3.0 Werafter terned hexosaminidase) is an enzyme which catalyses the hydrolysis of the terminal N-acetylglucosaminyl or N-acetylgaBactosWWpyl mMoieis$ from glycolipids and polysaccharides (Weissman et al, 1964;Sandhoff, 1970;Stirling, 1974) or from synthetic substrates i'n which the amino sugar is linked to a chromophoric group (Leaback & Walker, 1957, 1961). The enzyme exists in human and other mam.…”

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confidence: 99%

Purification and chemical characterization of human hexosaminidases A and B

Lee

Yoshida

1976

Biochemical Journal

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N-Acetyl-beta-hexosaminidases A and B were purified to homogeneity from human placenta. In the initial step of purification, the enzymes were adsorbed on concanavalin A-Sepharose 4B and eluted from the column with alpha-methyl D-mannosides. Subsequent purification steps included DEAE-cellulose column chromatography, QAE-Sephadex [diethyl-(2-hydroxypropyl)aminoethyl-Sephadex] column chromatography, Sephadex G-200 gel filtration and preparative disc polyacrylamide-gel electrophoresis, followed by another QAE-Sephadex chromatography for the hexosaminidase A preparation, and DEAE-cellulose column chromatography, calcium phosphate gel chromatography, Sephadex G-200 gel filtration, QAE-Sephadex chromatography and CM-cellulose chromatography for the hexosaminidase B preparation. The purified preparations, particularly hexosaminidase A, had significantly higher specific enzyme activities than previously reported. The preparations moved on polyacrylamide-gel electrophoresis as single protein bands, which also stained for enzyme activity. Sedimentation-equilibrium centrifugation indicated homogenous dispersion of the enzymes, and the molecular weight was estimated as about 110000 for both enzymes. Complete amino acid and carbohydrate compositions of the two isoenzymes were determined, and, in contrast with previous suggestions, no sialic acid was found in the enzymes.

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“…metric estimation of the liberated phenol. The development of a general method for the synthesis of alkyl and aryl N-acetyl-,-glucosaminides (Leaback & Walker, 1957) has extended the range of substrates available. This paper describes the kinetics of hydrolysis of an alkyl and four aryl N-acetyl-,-glucosaminides by enzymes from two sources.…”

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Studies on glucosaminidase. 2. Substrates for N-acetyl-β-glucosaminidase

Borooah

Leaback

Walker

1961

Biochemical Journal

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the oxygen uptake and acetoacetate oxidation when added alone or with fumarate, but not in the presence of a-oxoglutarate. The reasons for these differences are discussed. Anaerobically, relatively slight inhibitions of the reduction of acetoacetate were observed. 6. The oxidation of L(+)-p-hydroxybutyrate is inhibited by dinitrophenol, whereas that of the D(-)-form is not. This is related to the fact that only the L(+)-form requires conversion into the coenzyme A derivative. The differences in the behaviour of the Land D-forms towards dinitrophenol were used to examine the configuration of the P-hydroxybutyrate formed in sheep-heart muscle aerobically and anaerobically. In both cases the D-form only was found.

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958. The preparation and properties of acetochloroglucosamine and its use in the synthesis of 2-acetamido-2-deoxy-β-D-glucosides (N-acetyl-β-D-glucosaminides)

Cited by 69 publications

References 0 publications

N-Acetyl-Β-Glucosaminidase ACTIVITY IN SERUM DURING PREGNANCY

N-Acetyl-Β-Glucosaminidase ACTIVITY IN SERUM DURING PREGNANCY

Purification and chemical characterization of human hexosaminidases A and B

Studies on glucosaminidase. 2. Substrates for N-acetyl-β-glucosaminidase

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