Partition Paper Chromatography of Some Organic Acids

Opieńska-Blauth, J; Sakławska-Szymonowa, O.; Kański, M

doi:10.1038/168511b0

Cited by 19 publications

(3 citation statements)

References 3 publications

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“…Preparation of the hydrolysate for amino acid analysis, determination of the carboxyl and amino terminal amino acids of the purified RKNlysozyme were carried out according to standard procedures (3,4). Trytophan was determined by the methods of Spies & Chambers ( 5 ) and of Opienska et al (6). The presence of free sulfhy-dry1 groups was examined with 5,s dithiobis (2-nitrobenzoic acid) DTNB (7), while half cystine was estimated as cysteic acid after performic acid oxidation of the enzyme (8).…”

Section: Methodsmentioning

confidence: 99%

Structure‐activity Studies on Mammalian Tissue Lytic Enzymes: Chemical Characterization and Substrate Specificity of Rat Kidney Nuclear Lysozyme*

Raghunathan

Gurnani

1976

International Journal of Peptide and Protein Research

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Studies on the structure and substrate specificity of purified rat kidney nuclear (RKN) lysozyme are reported. The carboxyl and amino terminal residues of RKN‐lysozyme were found to be leucine and alanine respectively. The amino acid composition indicated similarities and differences as compared with that of hen egg white (HEW) lysozyme. There were alterations in the nine amino acid residues, Lys, His, Arg, Asp, Glu, Pro, 1/2 Cys, Tyr and Trp. The other nine residues were present in identical proportions to those of HEW‐lysozyme. The decrease in the arginine and aspartic acid residues was found to be compensated by the increase in the number of lysine, histidine and glutamic acid residues. The overall ratio of the acidic to basic amino acids has thus been conserved in the mammalian enzyme. In addition, RKN‐lysozyme contained decreased numbers of Trp, Tyr and 1/2 Cys, and increased numbers of proline residues as found in HEW‐lysozyme. RKN‐lysozyme did not cross react with heterologous antibodies produced against HEW‐lysozyme, and vice versa. RKN‐lysozyme showed distinct specificity towards the lysis of M. luteus. Against this substrate, it was three times more efficient than HEW‐lysozyme. It also cleaved E. coli B, but its efficiency was half as much as with M. luteus. However, it cleaved P. septica and B. subtilis at a rate similar to HEW‐lysozyme under identical conditions.

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Section: Methodsmentioning

confidence: 99%

Structure‐activity Studies on Mammalian Tissue Lytic Enzymes: Chemical Characterization and Substrate Specificity of Rat Kidney Nuclear Lysozyme*

Raghunathan

Gurnani

1976

International Journal of Peptide and Protein Research

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“…However, there is still a considerable volume of new literature on partition chromatography. It is carried out on columns of powdered cellulose (704) and silica gel (554) and on filter paper (103,201,259,271,282,670,741,805,840,841,951,953,960,1016,1072,1185,1188,1209,1217). Novel features include the direct application of acid protein hydrolyzates to the moistened paper, followed by drying in a stream of hot air (513), successive solvent development of biological materials without the removal of salts or proteins (863), and desalting of paper chromatograms by cutting off the starting spot (673).…”

Section: Alcoholsmentioning

confidence: 99%

Chromatography

Heftmanń¹

1962

Anal. Chem.

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“…The operation of paper chromatography is more versatile, however, as strips, strings (358), disks, and sheets of cellulose fiber may be used (174, 217, 250, 278, 349, 358), on a very' small scale (358), on a preparative scale (278) as with many' spots (74,217), and on a large scale (140) as by use of cellulose (60) or paper in columns (385). Separations may be improved by transverse development with a second solvent (two-way chromatography), and they may be Paper chromatography has been utilized for the separation of mixtures of monocarboxylic and of dicarboxylic acids (42,155,177,219,262,331,359), of aromatic acids (98), of hydroxy and keto acids (216), of ketohexonic acids (203), and of 2,4-dinitrophenylhydrazones of keto acids (5,71).…”

Section: Ion Exchangementioning

confidence: 99%