ISOLATION AND STRUCTURE OF URIDINE NUCLEOTIDE-PEPTIDES FROM AEROBACTER CLOACAE NRC 492

1963 ◽  
Vol 41 (4) ◽  
pp. 1065-1072 ◽  
Author(s):  
R. A. Anwar ◽  
C. Roy ◽  
R. W. Watson
Keyword(s):  
Lactic Acid ◽  
Amino Acid ◽  
Lithium Chloride ◽  
Paper Chromatography ◽  
High Voltage ◽  
Chloride Solutions ◽  
Uridine Nucleotide ◽  
Ethanol Extracts ◽  
Dowex 1 ◽  
High Voltage Electrophoresis

Four closely related uridine nucleotide-peptides isolated from ethanol extracts of penicillin-treated Aerobacter cloacae NRC 492 have been partially characterized. Fractionation of dialyzed extracts on Dowex-1-Cl columns with aqueous lithium chloride solutions, precipitation of the nucleotide-peptides with methanol–acetone, and further separation by paper chromatography and high voltage electrophoresis yielded (a) UDP-GNAc-lact.L-ala.D-glu.meso-dap.D-ala,* (b) UDP-GNAc-lact.L-ala.D-glu.meso-dap, (c) UDP-GNAc-lact.L-ala.D-glu., and (d) UDP-GNAc-lactic acid. The amino acid isomers were identified by micro-enzymic and chromatographic methods.

ISOLATION AND STRUCTURE OF URIDINE NUCLEOTIDE-PEPTIDES FROM AEROBACTER CLOACAE NRC 492

1963 ◽  
Vol 41 (1) ◽  
pp. 1065-1072 ◽  
Author(s):  
R. A. Anwar ◽  
C. Roy ◽  
R. W. Watson
Keyword(s):  
Lactic Acid ◽  
Amino Acid ◽  
Lithium Chloride ◽  
Paper Chromatography ◽  
High Voltage ◽  
Chloride Solutions ◽  
Uridine Nucleotide ◽  
Ethanol Extracts ◽  
Dowex 1 ◽  
High Voltage Electrophoresis

Four closely related uridine nucleotide-peptides isolated from ethanol extracts of penicillin-treated Aerobacter cloacae NRC 492 have been partially characterized. Fractionation of dialyzed extracts on Dowex-1-Cl columns with aqueous lithium chloride solutions, precipitation of the nucleotide-peptides with methanol–acetone, and further separation by paper chromatography and high voltage electrophoresis yielded (a) UDP-GNAc-lact.L-ala.D-glu.meso-dap.D-ala,* (b) UDP-GNAc-lact.L-ala.D-glu.meso-dap, (c) UDP-GNAc-lact.L-ala.D-glu., and (d) UDP-GNAc-lactic acid. The amino acid isomers were identified by micro-enzymic and chromatographic methods.

scholarly journals O-Methyl sugars in lipopolysaccharides of Rhodospirillacea. Identification of 3-O-methyl-d-mannose in Rhodopseudomonas viridis and of 4-O-methyl-d-xylose and 3-O-methyl-6-deoxy-d-talose in Rhodopseudomonas palustris respectively

1973 ◽  
Vol 135 (2) ◽  
pp. 293-297 ◽  
Author(s):  
Jürgen Weckesser ◽  
Hubert Mayer ◽  
Inge Fromme
Keyword(s):  
Mass Spectrometry ◽  
Paper Chromatography ◽  
High Voltage ◽  
Optical Rotation ◽  
Rhodopseudomonas Palustris ◽  
Rhodopseudomonas Viridis ◽  
Gram Negative ◽  
Optical Configuration ◽  
Alditol Acetates ◽  
High Voltage Electrophoresis

1. This paper deals with the identification of three O-methyl sugars in lipopolysaccharides isolated from strains of the Gram-negative photosynthetic family Rhodospirillaceae. In addition to the previously described 3-O-methyl-l-xylose, a second O-methyl sugar was encountered in the lipopolysaccharide of Rhodopseudomonas viridis F, namely 3-O-methyl-d-mannose. The lipopolysaccharides of two strains of Rhodopseudomonas palustris (strain 1e5 and 8/1) contain two O-methylsugars, 4-O-methyl-d-xylose and 3-O-methyl-6-deoxy-d-talose (d-acovenose). 4-O-Methyl-d-xylose, but not 3-O-methyl-6-deoxy-d-talose, could be identified in the lipopolysaccharides of the strains K/1 and 2/2 of the same species. 2. The O-methyl sugars described in this communication were isolated by paper chromatography and identified by g.l.c., paper chromatography, high-voltage electrophoresis and mass spectrometry. Besides the genuine sugars, their alditol acetates and their demethylated (parental) forms were investigated. Optical rotation measurements and, in one case, enzymic reactions were used to establish the optical configuration of the sugars under investigation.

Investigation of subtilisin digest of pepsin chain between half-cystines II and III

1981 ◽  
Vol 46 (3) ◽  
pp. 640-654
Author(s):  
Vladimír Kostka
Keyword(s):  
Amino Acid ◽  
Paper Chromatography ◽  
Sequential Analysis ◽  
Cysteine Residue ◽  
Amino Acid Sequences ◽  
Tryptic Digestion ◽  
Hydrolysis Of ◽  
Dowex 1 ◽  
Final Purification

Aminoethylated hog pepsin was subjected to tryptic digestion and the longest fragment, arising from cleavage at S-(β-aminoethyl)-cysteine residue No II and III was isolated from the digest. This fragment was subjected to additional cleavage with subtilisin and the digest resolved into crude fractions by chromatography on Dowex 1. The isolation and final purification of the peptides was carried out by paper electrophoreses and paper chromatography. By these methods 55 peptides were obtained which were subjected to sequential analysis by stepwise degradation. The amino acid sequences of these peptides and their position in the pepsin chain are given. These sequences provided overlaps for peptides obtained by hydrolysis of this part of the pepsin chain by other enzymes.

Specificity of γ-Glutamyl Cyclotransferase

1975 ◽  
Vol 53 (6) ◽  
pp. 706-712 ◽  
Author(s):  
Apolinary Szewczuk ◽  
George E. Connell
Keyword(s):  
Amino Acid ◽  
Carboxylic Acid ◽  
Synthetic Peptides ◽  
Terminal Position ◽  
Structural Requirement ◽  
Pig Liver ◽  
Racemic Mixtures ◽  
Dowex 1 ◽  
High Voltage Electrophoresis

Using the phthaloyl method, 18 γ-L-glutamyl peptides labelled with 14C in the N-terminal position have been synthesized. The products were isolated by simple procedures using a Dowex-1 column or high voltage electrophoresis. The synthetic peptides contain minor impurities of the corresponding D-glutamyl isomers. The proportion of D-isomer was determined by the use of glutamic decarboxylase, or by a new method using digestion with purified γ-glutamyl cyclotransferase and determination of the resulting 2-pyrrolidone-5-carboxylic acid (5-oxoproline). Evidence was obtained that γ-glutamyl cyclotransferase acts only on the L-form of γ-glutamyl substrates; the enzyme could, therefore, be used for preparation of γ-D-glutamyl peptides from their racemic mixtures. The specificity of γ-glutamyl cyclotransferase has been examined using pure enzyme prepared from pig liver, and extracts from tissues of rat and man. The basic structural requirement in substrates may be represented as γ-L-glutamyl—NH—CHR—COOH. The amino acid linked to the γ-glutamyl group must be in the L configuration.

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