A micro colorimetric determination of acidic glycosaminoglycans by two dimensional electrophoresis on a cellulose acetate strip

1973 ◽  
Vol 52 (2) ◽  
pp. 652-656 ◽  
Author(s):  
Ryuichiro Hata ◽  
Yutaka Nagai
Keyword(s):  
Cellulose Acetate ◽  
Colorimetric Determination ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Acidic Glycosaminoglycans ◽  
Dimensional Electrophoresis

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.

scholarly journals AUTOMATIC SELECTION OF TWO-DIMENSIONAL ELECTROPHORESIS GEL WITH LEAST GEOMETRIC DISTORTIONS

2010 ◽  
Vol 2 (1) ◽  
pp. 9-13
Author(s):  
Dalius Matuzevičius
Keyword(s):  
Quality Criterion ◽  
Horizontal Line ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Two Dimensional Electrophoresis ◽  
Geometric Distortions ◽  
Biochemical Experiment ◽  
Dimensional Electrophoresis ◽  
Selection Of

The paper presents an algorithm for automated selection of the highest quality two-dimensional gel electrophoresis image. The quality criterion is the amount of vertical geometric distortions of the gel. The aim is to select the least distorted gel from the group received during the same biochemical experiment. Vertical geometric distortions displace proteins of the same molecular mass from the horizontal line and have a greater impact on the determination of protein characteristics than horizontal distortions. After presenting algorithm for evaluation of distortions and selection of base gel results are compared to expert's made selections. If necessary, algorithm may be adapted for horizontal distortion evaluation.

Quantitative determination of haptoglobin glycoform variants in psoriasis

2010 ◽  
Vol 391 (12) ◽  
Author(s):  
Bernardetta Maresca ◽  
Luisa Cigliano ◽  
Maria M. Corsaro ◽  
Giuseppina Pieretti ◽  
Massimo Natale ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Immune Response ◽  
Extracellular Matrix ◽  
Quantitative Determination ◽  
Glycan Structure ◽  
Two Dimensional ◽  
Two Dimensional Electrophoresis ◽  
Dimensional Electrophoresis ◽  
Plasma Haptoglobin

AbstractHaptoglobin is an acute phase glycoprotein, secreted by hepatocytes and other types of cells including keratinocytes. Haptoglobin has been suggested to impair the immune response, inhibit gelatinases in the extracellular matrix and promote angiogenesis, but its role in psoriasis is obscure to date. Changes in haptoglobin glycan structure were observed in several diseases. The aim of this study was to investigate whether haptoglobin displays glycan variations in psoriasis. We found that the pattern of plasma haptoglobin glycoforms, following two-dimensional electrophoresis, exhibited significant quantitative differences in spot intensities between patients and controls. Quantitative and qualitative differences in glycan mass, between patients and controls, were found by mass spectrometry of glycopeptides from tryptic digests of protein isolated from both patients and controls. The number of distinct fucosylated glycoforms of peptides NLFLNHSENATAK and MVSHHNLTTGATLINEQWLLTTAK was higher in patients than in controls, but no fucosylated glycan was detected on peptide VVLHPNYSQ-VDIGLIK in either case. The number of peptides with distinct triantennary and tetraantennary glycans was higher in patients than in controls. Abundance or structure of specific glycans, which are present in haptoglobin from patients and are different or missing in normal haptoglobin, might be associated with disease activity.

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