Proteins of human urine. II. Identification by two-dimensional electrophoresis of a new candidate marker for prostatic cancer.

1982 ◽  
Vol 28 (1) ◽  
pp. 160-163 ◽  
Author(s):  
J J Edwards ◽  
N G Anderson ◽  
S L Tollaksen ◽  
A C von Eschenbach ◽  
J Guevara
Keyword(s):  
Sodium Dodecyl ◽  
Prostatic Hyperplasia ◽  
Prostatic Adenocarcinoma ◽  
Relative Molecular Mass ◽  
Urogenital System ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Candidate Marker ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis

Abstract A protein series common to the urine and prostatic tissue of 16 of 17 patients with prostatic adenocarcinoma has been identified by high-resolution two-dimensional gel electrophoresis. These proteins, designated PCA-1, have a relative molecular mass in sodium dodecyl sulfate of about 40000. Analyses of urines from eight age-matched controls, seven patients with other ty pes of urogenital malignancies, two patients with benign prostatic hyperplasia, and five patients with malignancies not associated with the urogenital system failed to show PCA-1 in the patterns. These preliminary findings suggest that this protein should be systematically investigated as a candidate marker for prostatic adenocarcinoma in man.

scholarly journals Red cell proteins. I. Two-dimensional mapping of human erythrocyte lysate proteins

Blood ◽  
1979 ◽  
Vol 53 (6) ◽  
pp. 1121-1132 ◽  
Author(s):  
JJ Edwards ◽  
NG Anderson ◽  
SL Nance ◽  
NL Anderson
Keyword(s):  
Human Erythrocyte ◽  
Sodium Dodecyl ◽  
Deae Cellulose ◽  
Cell Protein ◽  
Red Cell ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Mapping Techniques ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Dimensional Electrophoresis

Abstract Human erythrocyte lysate proteins were resolved into over 250 discrete spots by two-dimensional electrophoresis using isoelectric focusing in the first dimension and electrophoresis in the presence of sodium dodecyl sulfate, (SDS) in the second. The overwhelming excess of hemoglobin has made such analyses difficult in the past. However, with the ISO-DALT two-dimensional electrophoresis system, large numbers of red cell proteins can be mapped in the presence of hemoglobin. When hemoglobin and several other major proteins are removed by adsorption to DEAE-cellulose, additional minor components are seen, giving a total of over 275. With the use of purified preparations, the map positions of five cell enzymes or their subunits were determined: pyruvate kinase, catalase, glucose-6-phosphate dehydrogenase, hypoxanthine phosphoribosyltransferase, and carbonic anhydrase. The mapping techniques described complement and extend those traditionally used to find human red cell protein variants.

Evaluation of lipoproteins and apolipoproteins in serum of a Tangier patient by micro-scale two-dimensional electrophoresis.

1987 ◽  
Vol 33 (4) ◽  
pp. 468-472 ◽  
Author(s):  
T Manabe ◽  
S Visvikis ◽  
M F Dumon ◽  
M Clerc ◽  
G Siest
Keyword(s):  
Molecular Mass ◽  
Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Disease Patient ◽  
High Density Lipoproteins ◽  
Two Dimensional ◽  
High Concentration ◽  
Two Dimensional Electrophoresis ◽  
Micro Scale ◽  
Dimensional Electrophoresis

Abstract We examined lipoproteins and apolipoproteins in serum of a Tangier-disease patient. We used three different techniques of micro-scale two-dimensional electrophoresis: (a) no denaturants; (b) with sodium dodecyl sulfate (SDS) used only in the slab gel electrophoresis; (c) and with urea and a detergent used in isoelectric focusing and with SDS in slab gel electrophoresis. By technique a, an extremely low concentration of high-density lipoproteins (HDL) in the Tangier serum was seen, and lipoproteins that cannot form HDL complexes were detected as multiple spots in the acidic (pl 4 approximately 5) and relatively low apparent molecular mass (20,000 approximately 80,000) region. By technique b, Tangier low-molecular-mass lipoproteins were dissociated into their constituent apolipoproteins, and we observed a higher proportion of apoC-III, together with lower proportions of apoA-I and apoA-II, than in the normal HDL fraction. Technique c showed the total content of apolipoproteins in the whole Tangier serum, as several workers have reported. The presence of low-molecular-mass lipoproteins and a high concentration of apoC-III in this lipoprotein fraction characterized the Tangier serum.

scholarly journals Identification of protein disulphide-isomerase as a major acidic polypeptide in rat liver microsomal membranes

1983 ◽  
Vol 213 (1) ◽  
pp. 245-248 ◽  
Author(s):  
E N C Mills ◽  
N Lambert ◽  
R B Freedman
Keyword(s):  
Liver Enzyme ◽  
Rat Liver ◽  
Peptide Mapping ◽  
Bovine Liver ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Protein Disulphide Isomerase ◽  
Two Dimensional Electrophoresis ◽  
Microsomal Membranes ◽  
Dimensional Electrophoresis

Protein disulphide-isomerase was purified to homogeneity from rat liver by a rapid high-yielding procedure. Structural properties of the pure enzyme were very similar to those of the bovine liver enzyme purified by the same method. The purified rat liver enzyme was subjected to two-dimensional gel electrophoresis in the presence and in the absence of microsomal membranes, and shown to co-electrophorese with a major acidic polypeptide clearly identifiable in the two-dimensional electrophoretic profile of microsomal membranes. This identification was confirmed by peptide ‘mapping’ of the pure enzyme and of the defined spot from a two-dimensional electrophoresis gel.

Chromosomal locations of the structural genes for secalins in wild perennial rye (Secale montanum Guss.) and cultivated rye (S. cereale L.) determined by two-dimensional electrophoresis

1986 ◽  
Vol 28 (1) ◽  
pp. 76-83 ◽  
Author(s):  
P. R. Shewry ◽  
S. Parmar ◽  
N. Fulrath ◽  
D. D. Kasarda ◽  
T. E. Miller
Keyword(s):  
Molecular Weight ◽  
Storage Proteins ◽  
Seed Proteins ◽  
Relative Molecular Mass ◽  
Two Dimensional ◽  
Structural Genes ◽  
Substitution Lines ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Secale Montanum

The chromosomal locations of the structural genes for secalin storage proteins in Secale cereale and S. montanum were determined by electrophoresis of grain proteins from wheat–rye addition and substitution lines. The use of several different extraction procedures and high-resolution electrophoretic systems (one and two dimensional) enabled us to demonstrate that the genes for all the high molecular weight secalins are present on chromosome IRL, and for all the ω-secalins and at least some of the γ-secalins with a relative molecular mass (Mr) of 40 000 on chromosome IRS of both species. In contrast, the genes for the γ-secalins (Mr = 75 000) are located on 2RcS in S. cereale but 6Rm in S. montanum. These observations are discussed in relation to evolution of prolamins and their genes in Secale and related members of the Triticeae.Key words: Secale, rye, seed proteins, structural genes, two-dimensional electrophoresis.

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