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  Bifidus factor. V. The activity of α- and β-methyl-N-acetyl-d-glucosaminides

Rose, C. S., Kuhn, R., Zilliken, F., & Gyiirgy, P. (1945). Bifidus factor. V. The activity of α- and β-methyl-N-acetyl-d-glucosaminides. Archives of Biochemistry and Biophysics, 49(1), 123-129. doi:10.1016/0003-9861(54)90173-3.

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ArchBiochemBiophys_49_1954_123.pdf (Any fulltext), 370KB
 
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 Creators:
Rose, Catharine S., Author
Kuhn, Richard1, Author           
Zilliken, Friedrich, Author
Gyiirgy, Paul, Author
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1Max Planck Institute for Medical Research, Max Planck Society, ou_1125545              

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 Abstract: 1. β-Methyl-N-acetyl-d-glucosaminide is a growth factor for Lactobacillus bifidus var. Penn. The corresponding α-glucoside is inactive. 2. When mixtures of the inactive α-methyl-N-acetyl-d-glucosaminide and of the active β-isomer are used, the activity of the β-isomer is enhanced up to fivefold. 3. Other compounds containing NH-CO groups did not enhance the activity of β-methyl-N-acetyl-d-glucosaminide. In general, no or only very slight enhancement by the α-glucoside was observed when the β-glucoside was replaced by other substances with bifidus factor activity. 4. Lactobacillus bifidus var. Penn contains an enzyme that hydrolyzes and inactivates β-methyl-N-acetyl-d-glucosaminide but not the corresponding α-glucoside. In the presence of the α-glucoside the rate of hydrolysis of the β-glucoside was decreased. The observed in vitro effect did not seem sufficient to explain the microbiological response.

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Language(s): eng - English
 Dates: 1953-08-141945-03-01
 Publication Status: Issued
 Pages: 7
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 Table of Contents: -
 Rev. Type: Peer
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Title: Archives of Biochemistry and Biophysics
Source Genre: Journal
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Publ. Info: New York : Academic Press
Pages: - Volume / Issue: 49 (1) Sequence Number: - Start / End Page: 123 - 129 Identifier: ISSN: 0003-9861
CoNE: https://pure.mpg.de/cone/journals/resource/991042745826956