TWO-DIMENSIONAL ELECTROPHORESIS OF PROTEINS: USE OF CELLULOSE ACETATE MEMBRANE AND ISOELECTRIC FOCUSING GEL

1983 ◽  
pp. 343-352
Keyword(s):  
Cellulose Acetate ◽  
Isoelectric Focusing ◽  
Cellulose Acetate Membrane ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Electrophoresis Of Proteins

Two-dimensional electrophoresis of proteins with a different approach to isoelectric focusing

The Analyst ◽  
1994 ◽  
Vol 119 (6) ◽  
pp. 1341-1344 ◽  
Author(s):  
S. M. Saqlan Naqvi ◽  
V. Cengiz Özalp ◽  
H. Avni Öktem ◽  
Meral Yücel
Keyword(s):  
Isoelectric Focusing ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Electrophoresis Of Proteins

Analytical electrofocusing and two-dimensional electrophoresis of proteins extracted from the mycelia of aggressive and nonaggressive strains of Ophiostoma ulmi

1986 ◽  
Vol 64 (9) ◽  
pp. 2073-2081 ◽  
Author(s):  
Robert S. Jeng
Keyword(s):  
Dutch Elm Disease ◽  
Two Dimensional ◽  
Polyacrylamide Gels ◽  
Ophiostoma Ulmi ◽  
Two Dimensional Electrophoresis ◽  
Coomassie Blue ◽  
Isoelectric Points ◽  
Additional Protein ◽  
Dimensional Electrophoresis ◽  
Electrophoresis Of Proteins

Soluble mycelial proteins from Ophiostoma ulmi (Buism.) Nannf., the causal agent of Dutch elm disease, were separated by analytical electrofocusing and two-dimensional electrophoresis in polyacrylamide gels. Results showed the aggressive and nonaggressive strains of this pathogen each had about 60 Coomassie blue stained bands having isoelectric points from 3 to 7. Both strains of this fungus had their own characteristic electrofocusing patterns. Nonaggressive isolate S116, for example, lacked two protein bands, one near the anode and one near the cathode, but it had five additional protein bands distributed from pH 4 to 6. Two-dimensional electrophoresis of total soluble proteins depicted that there were 36 proteins found to be specific for the nonaggressive isolate S116 and 12 proteins for the aggressive isolate RR2.

Direct quantitation of glycosaminoglycans in 2 mL of urine from patients with mucopolysaccharidoses.

1981 ◽  
Vol 27 (1) ◽  
pp. 124-128 ◽  
Author(s):  
R W Burlingame ◽  
G H Thomas ◽  
R L Stevens ◽  
K Schmid ◽  
H W Moser
Keyword(s):  
Cellulose Acetate ◽  
Alcian Blue ◽  
Keratan Sulfate ◽  
Two Dimensional ◽  
Chondroitinase Abc ◽  
Two Dimensional Electrophoresis ◽  
Specific Degradation ◽  
Dimensional Electrophoresis

Abstract Glycosaminoglycans in urine from patients representing the major different mucopolysaccharidoses were separated and measured by use of a procedure that requires only 2 mL of urine. The compounds were resolved by two-dimensional electrophoresis on cellulose acetate plates and made visible by staining with Alcian Blue. They were identified by co-migration with standard glycosaminoglycans, by digestion with specific glycosidases, and by specific degradation with HNO2. They were quantitated by comparing the absorbance of eluates of the stained spots to appropriate standard curves for each glycosaminoglycan. This study revealed additional findings. About half of the patients excreted small amounts of heparin. Further, the keratan sulfate in samples from Morquio's disease patients migrated differently from authentic keratan sulfate unless digested with chondroitinase ABC. Our results for these diseases are in harmony with earlier reports.

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