Procedure for determination of d-amino acids

Larson, David M.; Snetsinger, D. C.; Waibel, P. E.

doi:10.1016/0003-2697(71)90429-5

Cited by 30 publications

(11 citation statements)

References 9 publications

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“…The correction for destruction during hydrolysis was based on the analysis of mixtures of known quantities of authentic amino acids and amino sugars which were hydrolyzed under identical conditions as samples. The configuration of alanine was determined with D-alanine oxidase (20). The reaction was monitored with the amino acid analyzer.…”

Section: Methodsmentioning

confidence: 99%

Biochemical and immunochemical properties of the cell surface of Renibacterium salmoninarum

Fiedler¹,

Draxl²

1986

J Bacteriol

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The biochemical composition of the cell envelope of Renibacterium salmoninarum was investigated in a total of 13 strains isolated from different salmonid fish species at various geographicil locations of the United States, Canada, and Europe. A marked similarity with the type strain R. salmoninarum ATCC 33209 was found both in the peptidoglycan and the cell wall polysaccharide. The primary structure of the peptidoglycan was found to be consistent with lysine in the third position of the peptide subunit, a glycyl-alanine interpeptide bridge between lysine and D-alanine of adjacent peptide subunits, and a D-alanine amide substituent at the a-carboxyl group of D-glutamic acid in position 2 of the peptide subunit. The cell wall polysaccharide contained galactose as the major sugar component which was accompanied by rhamnose, N-acetylglucosamine, and Nacetylfucosamine. The polysaccharide amounted to more than 60% of the dry weight of the cell walls. It was found to be covalently linked to the peptidoglycan and was released by hot formamide treatment. On gel filtration chromatography the extracted polysaccharide behaved like a homogeneous polymeric compound. The purified cell wall polysaccharide showed antigenic activity with antiserum obtained by immunization of rabbits with heat-inactivated trypsinized cells of R. salmoninarum. Immunoblotting experiments with nontrypsinized cell walls and antisera raised against R. salmoninarum cells revealed that antigenic proteins were attached to the cell walls.

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Section: Methodsmentioning

confidence: 99%

Biochemical and immunochemical properties of the cell surface of Renibacterium salmoninarum

Fiedler¹,

Draxl²

1986

J Bacteriol

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“…Spots were localized by ninhydrin reaction and isolated from fluorescamine-stained [9] chromatograms for further determination. The conformation of alanine was determined using D-alanine oxidase [10]. The reaction was monitored using the amino acid analyzer.…”

Section: Methodsmentioning

confidence: 99%

Murein type and polysaccharide composition of cell walls fromRenibacterium salmoninarum

Kusser

Fiedler

1983

FEMS Microbiology Letters

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The primary structure of the murein of Renibacterium salmoninarum ATCC33209 was determined. It contained lysine in the third position of the peptide subunit, a glycyl‐alanine interpeptide bridge between lysine and the d‐alanine of adjacent peptide subunits and a d‐alanine‐amide substitution at the α‐carboxyl group of d‐glutamic acid in position 2 of the peptide side chain. Cell walls contained a considerable amount of polysaccharide with galactose as major sugar component. In addition N‐acetyl‐glucosamine, rhamnose and N‐acetyl‐fucosamine were detected.

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“…HTrp-OH [8] (27.8 g, 136 mmol) in 300 ml dioxane and 136 ml1N NaOH was reacted with Z-Phe-ONSu [7] (27 g, 68 mmol). The reaction was allowed to proceed for 12 hr a t room temperature; then the bulk of dioxane was extracted twice with EtOAc.…”

Section: Synthesis Of Somatostatin 21mentioning

confidence: 99%

New synthesis of somatostatin according to the S‐tert‐butylthiocysteine procedure

et al. 1981

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SynopsisTo exemplify the usefulness of the S-tert-butylthio group for a reversible blocking of the cysteine thiol function in peptide synthesis, fully protected dihydrosomatostatin was prepared by the fragment-condensation procedure. The experimental results confirm the excellent stability of the asymmetric disulfide under the normal conditions of peptide synthesis and prove that the selective, acid-catalyzed nucleophil removal-as well as by mercaptans-of the 2-nitrophenylsulfenyl group proceeds smoothly in the presence of this thiol protection.Thus, the strategy of overall acid-labile side-chain protection in combination with the N"-2-nitrophenylsulfenyl group for the chain-elongation steps can be successfully applied to the synthesis of cysteine-containing peptides using their S-tert -butylthio derivatives. Removal of the acid-labile groups, followed by reductive cleavage of the asymmetric disulfides and successive air oxidation, allowed a clean conversion of protected dihydrosomatostatin into somatostatin a t a high degree of purity and in good yields. INTRODUCTIONThe great demand for new thiol-protecting groups, highly stable in the normal operating conditions of peptide synthesis and removable by mild and, in regard to other known cysteine derivatives, selective methods led Wunsch and Spangenberg' to propose the S-tert-butylthio function as a group fulfilling above requirements. This asymmetric disulfide is, in fact, resistant to acid-and base-induced disproportionation, and it is cleaved by mild reagents such as mercaptans.' Because of our positive experiences (Ref. 2, p. 792, and unpublished results) with this protecting group, a new synthesis of the clinically important hypothalamic hormone s~rnatostatin:~-~ was performed to further investigate the potential properties of the Stert-butylthio group in the course of peptide synthesis.* Some of the results of this paper were presented in a preliminary communication a t the Second FRG-USSR Symposium on Chemistry of Peptides and Proteins, Grainau-Eibsee/ Bavaria, May [24][25][26][27] 1978: Moroder, L., Musiol, d., Scharf, R., and Wunsch, E. (1978) in Proceedings, pp. 24-25.t To whom correspondence should be addressed.Biopolymers, Vol. 20.17-37 (1981 EXPERIMENTALMelting points were determined on a Tottoli capillary melting-point apparatus and are uncorrected. Optical rotations were measured in a jacketed 1-dm cell on a Perkin Elmer model 141 polarimeter. The acid hydrolyses were conducted in 6M HC1 a t 110°C for 20 hr in the presence of thioglycolic acid for Trp-containing peptides6 in evacuated, sealed ampules. D-Amino acid oxidase (Boehringer, Mannheim, Lot No. 1419221) digestion was carried out according to the procedure of Larson et al.7 Aminopeptidase M (Sigma, L-6007, Lot No. 67C-85001) digestion was performed in Tris buffer, pH 7.8, a t 37°C for 20 hr. Amino acid analyses were obtained on the Beckman amino acid analyzer equipped with automatic digital integrator (models 120 B and 125). The purity tests for the single compounds (25-50 pg) were car...

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Procedure for determination of d-amino acids

Cited by 30 publications

References 9 publications

Biochemical and immunochemical properties of the cell surface of Renibacterium salmoninarum

Biochemical and immunochemical properties of the cell surface of Renibacterium salmoninarum

Murein type and polysaccharide composition of cell walls fromRenibacterium salmoninarum

New synthesis of somatostatin according to the S‐tert‐butylthiocysteine procedure

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