Methods for Computer Analysis and Comparison of Two-Dimensional Protein Patterns Obtained by Electrophoresis

1987 ◽  
pp. 529-537 ◽  
Author(s):  
Reinhold C. Mann ◽  
Betty K. Mansfield ◽  
James K. Selkirk
Keyword(s):  
Computer Analysis ◽  
Two Dimensional ◽  
Protein Patterns

Two-dimensional computer analysis of GaAs MESFETs

1993 ◽  
Vol 36 (4) ◽  
pp. 547-552 ◽  
Author(s):  
Xiaoqi Dong ◽  
M. El Nokali
Keyword(s):  
Computer Analysis ◽  
Two Dimensional

Variation in goat fibre protein

1989 ◽  
Vol 40 (3) ◽  
pp. 675 ◽  
Author(s):  
DJ Tucker ◽  
AHF Hudson ◽  
A Laudani ◽  
RC Marshall ◽  
DE Rivett
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Apparent Molecular Weight ◽  
Wool Fibre ◽  
Two Dimensional ◽  
Protein Patterns ◽  
Cashmere Goats

The proteins from a range of cashmere, mohair, angoratcashmere crossbred and wool fibre samples were extracted at pH 8 with 8 M urea containing dithiothreitol, and were then radiolabelled by S-carboxymethylation using iodo(2-14C) acetate. The proteins from each sample were examined by two dimensional polyacrylamide gel electrophoresis in which the separation in the first dimension was according to charge at pH 8.9 and in the second dimension according to apparent molecular weight in the presence of sodium dodecyl sulfate. After electrophoresis the proteins were detected by fluorography. Protein differences in keratin samples from some individual goats existed, although the overall protein patterns were similar. None of the differences were consistent with any one goat fibre type. The protein patterns obtained for fibre samples from individual cashmere goats showed some differences when compared to those found for commercial blends from the same country of origin, indicating that blending can mask any animal-to-animal variation. While the electrophoretic technique does not unequivocally distinguish between cashmere, mohair and angora/cashmere crossbred fibres it does differentiate between wool and goat fibres.

Systematic characterization of human prostatic fluid proteins with two-dimensional electrophoresis.

1984 ◽  
Vol 30 (12) ◽  
pp. 2026-2030 ◽  
Author(s):  
Y C Tsai ◽  
H H Harrison ◽  
C Lee ◽  
J A Daufeldt ◽  
L Oliver ◽  
...  
Keyword(s):  
Benign Prostatic Hyperplasia ◽  
Serum Proteins ◽  
Prostatic Hyperplasia ◽  
Affinity Column ◽  
Two Dimensional ◽  
Differential Analysis ◽  
Protein Patterns ◽  
Prostatic Fluid ◽  
Serum Components

Abstract We present a systematic analysis of human prostatic fluid with two-dimensional gel electrophoresis (the ISO-DALT system) and a characterization of normal and disease-related protein patterns. A reference map for prostatic fluid proteins was established by analysis of pooled prostatic fluids from 80 men (age less than or equal to 50 years) without prostatic lesions. Proteins in prostatic fluid that share immunogenicity with serum proteins were identified by use of antibody to whole human-serum protein in an affinity-column fractionation of a reference pool and differential analysis of the absorbed (serum components) and unabsorbed (non-serum components) fractions. Individual prostatic fluids from 30 patients (eight with prostatic cancer, 10 with prostatitis and benign prostatic hyperplasia, six with benign prostatic hyperplasia alone, and six with asymptomatic chronic prostatitis) were scored qualitatively with respect to the presence or absence of 57 major prostatic fluid proteins. Statistically significant, disease-correlated alterations were observed for at least eight of the proteins so scored.

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