scholarly journals Isolation of bacilysin and a new amino acid from culture filtrates of Bacillus subtilis

1970 ◽  
Vol 118 (4) ◽  
pp. 557-561 ◽  
Author(s):  
J. E. Walker ◽  
E. P. Abraham

1. Bacilysin, a labile dipeptide antibiotic that lyses growing staphylococci, was isolated from culture fluids of Bacillus subtilis by a process giving higher yields than those previously obtained. 2. The process involves adsorption on a cation-exchange resin and elution with aqueous trimethylamine, separation from neutral amino acids and glutamic acid by chromatography on DEAE-Sephadex at pH8.7 and separation from other neutral peptides by chromatography in aqueous propan-2-ol on Sephadex G-25. 3. A new amino acid, which is chemically related to bacilysin, was isolated from the fraction containing neutral amino acids. 4. Two substances that yield alanine on hydrolysis, in addition to bacilysin, were obtained from the neutral peptide fraction.

2013 ◽  
Vol 699 ◽  
pp. 770-774
Author(s):  
Jian Hua Yi ◽  
Mei Li Li ◽  
Zhen Bao Zhu

In order to inhibit non-enzymatic browning in clarified Fuji apple juice during storage, four kinds of cation exchange resins were compared for their abilities to exchange and remove amino acids, the reaction substrates of non-enzymatic browning in apple juice. The favorite resin, LSI-100, was screened to carry out static and dynamic adsorption experiments. The results showed that LSI-100 cation exchange resin had the best capacity for adsorption and removal amino acids. The equilibrium time of LSI-100 resin for amino acids was 3.5h.And the isotherm of LSI-100 resin could be described by Freundlich at 20°C. Additionally, the flow rates, temperature and concentrations of amino acids in apple juice affected the dynamic kinetic curves of LSI-100 cation exchange resin and the better dynamic exchange and adsorption parameters were as follows: flow rate 4BV/h, temperature 50°C,and amino acid concentration 30mg/100g apple juice.


Radiocarbon ◽  
1989 ◽  
Vol 31 (03) ◽  
pp. 247-253 ◽  
Author(s):  
I A Law ◽  
R E M Hedges

A semi-automated continuous-flow system used to process archaeological bone to purified gelatin or amino acids for 14C dating is described. Powdered bone is retained in flow cells specifically designed to permit the sequential leaching of the bone with acid, alkali and water. Crude collagen obtained by this process is gelatinized, and than either purified directly using a macroporous cation exchange resin (BioRad AGMP-50), or hydrolyzed and the amino acids desalted on BioRad 50W-X8 resin. When compared with previous methods used by the laboratory, the new method allows more samples to be treated to a higher degree of purification. Examples of dates obtained on “standard” bones are presented, and confirm that no contamination is introduced from the components used in the new process.


1967 ◽  
Vol 102 (3) ◽  
pp. 801-814 ◽  
Author(s):  
M. C. Corfield ◽  
J. C. Fletcher ◽  
A. Robson

1. A tryptic digest of the protein fraction U.S.3 from oxidized wool has been separated into 32 peptide fractions by cation-exchange resin chromatography. 2. Most of these fractions have been resolved into their component peptides by a combination of the techniques of cation-exchange resin chromatography, paper chromatography and paper electrophoresis. 3. The amino acid compositions of 58 of the peptides in the digest present in the largest amounts have been determined. 4. The amino acid sequences of 38 of these have been completely elucidated and those of six others partially derived. 5. These findings indicate that the parent protein in wool from which the protein fraction U.S.3 is derived has a minimum molecular weight of 74000. 6. The structures of wool proteins are discussed in the light of the peptide sequences determined, and, in particular, of those sequences in fraction U.S.3 that could not be elucidated.


2009 ◽  
Vol 44 (13) ◽  
pp. 3075-3087 ◽  
Author(s):  
Hidetada Nagai ◽  
Kazuhiro Hasegawa

1990 ◽  
Vol 29 (5) ◽  
pp. 849-857 ◽  
Author(s):  
Susan R. Dye ◽  
Joseph P. DeCarli ◽  
Giorgio Carta

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