scholarly journals Width Based Characterization of Chromatographic Peaks: Beyond Height and Area

2017 ◽  
Vol 89 (7) ◽  
pp. 3893-3900 ◽  
Author(s):  
Akinde F. Kadjo ◽  
Hongzhu Liao ◽  
Purnendu K. Dasgupta ◽  
Karsten G. Kraiczek
Keyword(s):  
Chromatographic Peaks

Isolation and preliminary characterization of a fraction of bilirubin in serum that is firmly bound to protein.

1982 ◽  
Vol 28 (4) ◽  
pp. 629-637 ◽  
Author(s):  
J J Lauff ◽  
M E Kasper ◽  
T W Wu ◽  
R T Ambrose
Keyword(s):  
Azo Dyes ◽  
Diazonium Salt ◽  
Visible Spectrum ◽  
Strong Acid ◽  
The Other ◽  
Direct Reaction ◽  
Fraction Absorbed ◽  
Chromatographic Peaks ◽  
Liquid Chromatographic

Abstract We have isolated from pathological sera a bilirubin fraction (delta) that is very tightly, if not covalently, bound to protein, most likely albumin. This delta fraction absorbed at a lambda max of 433 nm in the visible spectrum, between the lambda max of unconjugated (alpha) and that of conjugated (Bc) bilirubin when measured in solutions containing albumin. However, unlike the other bilirubin species, this fraction could not be separated from the proteins in serum by exhaustive ultrafiltration in the presence of caffeine/benzoate solution. In the Jendrassik-Grof diazo procedure for bilirubin analysis, the delta fraction gave a large direct reaction (76-89% of the total reaction). Yet, when relatively hydrophobic azo dyes were formed by reaction of the delta fraction with the diazonium salt of dichloroaniline, only 50% of the dyes were extractable from aqueous solution. On chromatography the rest remained associated with protein. Of the extractable dye, more than 70% was accounted for by two liquid-chromatographic peaks with retentions identical with those of azo dyes formed from unconjugated bilirubin. This delta fraction was not appreciably separated from protein by treatment with strong acid or base, or by prolonged digestion with various enzymes. Finally, in a highly denaturing solvent (urea/mercaptoethanol), this fraction was not dialyzable through a membrane with a 12 000-dalton cutoff.

Computer characterization of chromatographic peaks by plate height and higher central moments

1969 ◽  
Vol 41 (7) ◽  
pp. 889-892 ◽  
Author(s):  
Elimelech. Grushka ◽  
Marcus N. Myers ◽  
Paul D. Schettler ◽  
J. Calvin. Giddings
Keyword(s):  
Plate Height ◽  
Central Moments ◽  
Chromatographic Peaks

Morphological Characterization of Mycobacteriophage R1

1974 ◽  
Vol 32 ◽  
pp. 254-255
Author(s):  
B. L. Soloff ◽  
T. A. Rado
Keyword(s):  
Carbon Source ◽  
Stationary Phase ◽  
Growth Phase ◽  
Minimal Medium ◽  
Morphological Characterization ◽  
Logarithmic Growth Phase ◽  
Complete Lysis ◽  
Lysogenic Culture ◽  
Logarithmic Growth

Mycobacteriophage R1 was originally isolated from a lysogenic culture of M. butyricum. The virus was propagated on a leucine-requiring derivative of M. smegmatis, 607 leu−, isolated by nitrosoguanidine mutagenesis of typestrain ATCC 607. Growth was accomplished in a minimal medium containing glycerol and glucose as carbon source and enriched by the addition of 80 μg/ ml L-leucine. Bacteria in early logarithmic growth phase were infected with virus at a multiplicity of 5, and incubated with aeration for 8 hours. The partially lysed suspension was diluted 1:10 in growth medium and incubated for a further 8 hours. This permitted stationary phase cells to re-enter logarithmic growth and resulted in complete lysis of the culture.

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