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Structure and function of proteins of the phosphotransferase system and of 6-phospho-β-glycosidases in Gram-positive bacteria (1993)

Hengstenberg, Wolfgang ; Kohlbrecher, Detlef ; Witt, Ellen ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

FEMS microbiology reviews 12 (1993), S. 0

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ISSN: 1574-6976

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Biology

Notes: Abstract: New information about the proteins of the phosphotransferase system (PTS) and of phosphoglycosidases of homofermentative lactic acid bacteria and related species is presented. Tertiary structures were elucidated from soluble PTS components. They help to understand regulatory processes and PTS function in lactic acid bacteria. A tertiary structure of a membrane-bound enzyme II is still not available, but expression of Gram-positive genes encoding enzymes II can be achieved in Escherichia coli and enables the development of effective isolation procedures which are necessary for crystallization experiments. Considerable progress was made in analysing the functions of structural genes which are in close vicinity of the genes encoding the sugar-specific PTS components, such as the genes encoding the tagatose-6-P pathway and the 6-phospho-β-glycosidases. These phosphoglycosidases belong to a subfamily of the β-glycosidase family I among about 300 different glycosidases. The active site nucleophile was recently identified to be Glu 358 in Agrobacteriumβ-glucosidase. This corresponds to Glu 375 in staphylococcal and lactococcal 6-phospho-β-galactosidase. This enzyme is inactivated by mutating Glu 375 to Gln. Diffracting crystals of the lactococcal 6-P-β-galactosidase allow the elucidation of its tertiary structure which helps to derive the structures for the entire glycosidase family 1. In addition, a fusion protein with 6-phospho-β-galactosidase and staphylococcal protein A was constructed.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1574-6976.1993.tb00016.x

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Sex differences in muscarinic receptor binding after chronic ethanol administration in the rat (1986)

Witt, Ellen D. ; Mantione, Charles R. ; Hanin, Israel

Springer

Psychopharmacology 90 (1986), S. 537-542

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ISSN: 1432-2072

Keywords: Chronic ethanol administration ; Sex differences ; Muscarinic receptor binding

Source: Springer Online Journal Archives 1860-2000

Topics: Medicine

Notes: Abstract Male and female rats were administered ethanol (5% v/v) in a liquid diet for 18 weeks. Pair-fed control animals were fed the same diet except that dextrose was substituted isocalorically for ethanol. Normal controls received a commercial laboratory chow for the same duration. Results showed that, in females, chronic ingestion of an ethanol liquid diet significantly increased the number of muscarinic receptor binding sites compared to both control groups. In contrast, for males, there was no significant difference in the mean number of binding sites among the treatment groups. Furthermore, the mean maximum number of binding sites for males and females varied across brain areas. Males had a significantly greater number of receptor binding sites than females in the striatum, while females had a greater number in the cortex. It was suggested that the geuder differences observed in the present study could be mediated by hormonal effects on central muscarinic functioning.