scholarly journals Studies on the analysis of environmental pollutants by micellar electrokinetic chromatography/Studies on improvement for analyses of some poisons in blood and urine, and estimation of bloodstain age/Development of novel group-specific adsorbents for high-performance affinity chromatography and their applications to a system for selective on-line enrichment and separation of bioactive peptides

1999 ◽  
Vol 48 (5) ◽  
pp. 523-530 ◽  
Author(s):  
Sahori TAKEDA ◽  
Toshiyasu MATSUOKA ◽  
Kimihiro ISHIMURA ◽  
Shigeru AMEMIYA
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
Micellar Electrokinetic Chromatography ◽  
Bioactive Peptides ◽  
Environmental Pollutants ◽  
Electrokinetic Chromatography ◽  
High Performance Affinity Chromatography ◽  
On Line

Liver- and bone-derived isoenzymes of alkaline phosphatase in serum as determined by high-performance affinity chromatography

1990 ◽  
Vol 36 (2) ◽  
pp. 240-246 ◽  
Author(s):  
D J Anderson ◽  
E L Branum ◽  
J F O'Brien
Keyword(s):  
Alkaline Phosphatase ◽  
Affinity Chromatography ◽  
High Performance ◽  
Bone Alkaline Phosphatase ◽  
Phosphate Solution ◽  
Serum Samples ◽  
High Performance Affinity Chromatography ◽  
Nitrophenyl Phosphate ◽  
On Line ◽  
Two Peaks

Abstract To separate liver and bone alkaline phosphatase (ALP) isoenzymes in human serum, we used high-performance affinity chromatography (HPAC) on a column of wheat-germ lectin conjugated to 7-microns-diameter silica particles and an eluent containing N-acetyl-D-glucosamine (NAG). On-line spectrophotometric detection of ALP involved pumping diethanolamine-buffered p-nitrophenyl phosphate solution post-column. Bone and liver isoenzymes could be separated into two peaks with only 10% overlap when an exponential gradient was used. A linear-step gradient separated 80.9% of liver ALP and 91.6% of bone ALP in two distinct peaks. True bone and liver ALP peak areas for the linear-step gradient were determined by using correction factors, because each peak contained a co-eluted portion of the other ALP isoenzyme. The detection limit improved 10-fold over those of other techniques for ALP isoenzymes, owing to the relatively large sample that could be applied to the column. Correlation with a urea-inactivation procedure was reasonable for patients' serum samples (r = 0.98 and 0.79 for liver ALP and bone ALP, respectively).

A new method for the analysis of plasmin and plasminogen. Application of high-performance affinity chromatography.

1985 ◽  
Vol 16 (1) ◽  
pp. 23-25
Author(s):  
Kenichi KASAI ◽  
Kiyohito SHIMURA ◽  
Naofumi ITO ◽  
Kohji NOGUCHI ◽  
Mutsuyoshi KAZAMA
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
New Method ◽  
High Performance Affinity Chromatography

Affinity surfactants as reversibly bound ligands for high-performance affinity chromatography

1988 ◽  
Vol 171 (2) ◽  
pp. 411-418 ◽  
Author(s):  
J.L. Torres ◽  
R. Guzman ◽  
R.G. Carbonell ◽  
P.K. Kilpatrick
Keyword(s):  
Affinity Chromatography ◽  
High Performance ◽  
High Performance Affinity Chromatography
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