Hemmung der Neuraminidase aus Vibrio cholerae

Mohr, Elisabeth

doi:10.1515/znb-1960-0906

Cited by 18 publications

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“…To test the number of accessible active sites, a combination of enzymesulphated glycopeptide complex with a competitive inhibitor of the enzyme was examined. In these experiments, neuraminidase from V. cholerae was used, since N-acetylneuraminic acid acts as a competitive inhibitor with respect to N-acetylneuraminyllactose (Mohr, 1960). The K1 value calculated from Dixon's plot of 1/v against [I] at different substrate concentrations (Dixon & Webb, 1964b) was 1.4 x 10-2M (Fig.…”

Section: Inhibition Of Neuraminidase-catalysed Release Of Sialic Acidmentioning

confidence: 99%

Neuraminidase inhibition by chemically sulphated glycopeptides

Mian¹,

Anderson²,

Kent³

1979

Biochemical Journal

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Chemically sulphated glycopeptides (derived from pig duodenal mucosa) inhibited Clostridium perfringens neuraminidase (EC 3.2.1.18) activity in a pH-dependent manner. Analysis of inhibition kinetics data indicated that, although the enzyme inhibition could not be categorized into any of the classical types of inhibition, it could be interpreted as a function of the size and shape of the substrates used. The enzyme activity was inhibited by 86% and 40% when tested with bovine submaxillary-gland mucin (mol. wt. 4 x 10(5)-40 x 10(5) and N-acetylneuraminyl-lactose (mol. wt. 633) as substrates respectively. Presence of sulphated glycopeptide did not affect the binding of N-acetylneuraminic acid (mol. wt. 309), a competitive inhibitor of Vibrio cholerae neuraminidase, to the enzyme active site. The enzyme inhibition was thus considered to be due to steric hindrance as a consequence of the non-specific interactions between the enzyme molecule and polyanionic sulphated glycopeptide affecting the differential accessibility of the substrate molecules to the enzyme active site. The enzyme-inhibitor interaction could be suppressed by rapid and many-fold dilution of the reaction mixture, by concurrent addition of the inactive enzyme or by partial removal of the sulphate esters from the sulphated glycopeptide molecule by the action of Helix pomatia arylsulphatase (EC 3.1.6.1).

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Section: Inhibition Of Neuraminidase-catalysed Release Of Sialic Acidmentioning

confidence: 99%

Neuraminidase inhibition by chemically sulphated glycopeptides

Mian¹,

Anderson²,

Kent³

1979

Biochemical Journal

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Temperature effect on the single and double hydrogen atom transfer reactions in o‐, m‐and p‐toluic acid butyl esters

Tajima

Yanagisawa

Azami

et al. 1980

Org. Mass Spectrom.

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INTRODUCXIONBoth single and double hydrogen atom transfer reactions (1) and (2) paper, it has been reported4 from the m a s spectra of alkyl o-hydroxybenzoates (alkyl salicylates) and alkyl p-hydroxybenzoates that the intramolecular hydrogen bond' (interaction between the hydrogen atom in the hydroxyl group and the oxygen atom in the carboxyl group) may prevent the second hydrogen atom transfer.In the present paper, the temperature effect on the abundances of the rnlz 137 and mlz 136 ions generated by the reactions (2) and (1) RESULTS AND DISCUSSIONIn the mass spectra of alkyl p-hydroxybenzoates, both rnlz 139 and rnlz 138 ions from reactions (2) and (1) were found? In contrast, only the single hydrogen atom transferred ion at mlz 138 was found in the spectra of alkyl salicylates, which have a hydroxyl group with a strong electron-donating property at the ortho p~s i t i o n .~In the case of toluic acid butyl esters, which have a methyl group with a weaker electron-donating property, the abundances of rearrangement ions caused by reactions (1) and (2) which occur at rnlz 136 and m/z 137 became quite intense. The mass spectra of the compounds studied are shown in Table 1

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