Corticosteroid Induced Alkaline Phosphatase: Cellular Location, Biochemical Characterization and Comparison to Intestinal Alkaline Phosphatase of the Dog (Amino Acid, Monoclonal Antibody, Peptide Mapping, Carbohydrate, N-Terminal)
Sanecki, Robin Kenneth
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https://hdl.handle.net/2142/71338
Description
Title
Corticosteroid Induced Alkaline Phosphatase: Cellular Location, Biochemical Characterization and Comparison to Intestinal Alkaline Phosphatase of the Dog (Amino Acid, Monoclonal Antibody, Peptide Mapping, Carbohydrate, N-Terminal)
Author(s)
Sanecki, Robin Kenneth
Issue Date
1986
Department of Study
Veterinary Medical Science
Discipline
Veterinary Medical Science
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Veterinary Science
Abstract
The purpose of the research was to identify the subcellular location of the corticosteroid-induced isoenzyme of alkaline phosphatase (SIALP) in the liver, purify the SIALP, the intestinal isoenzyme of alkaline phosphatase (IALP) and the hepatic isoenzyme of alkaline phosphatase (LALP), develop an effective means of purification for IALP and SIALP, and characterize the purified isoenzymes. The location of the SIALP was determined to be the hepatocyte membranes which comprise the bile canaliculi of the liver. Four monoclonal antibodies against IALP were produced which cross reacted with SIALP but not with LALP. These were fused to cyanogen bromide activated sepharose and used to develop a rapid purification procedure which dramatically increased the yield of IALP and SIALP over the conventional chromatography techniques used to purify LALP. Results of amino acid analysis, peptide mapping, N-terminal sequencing of the first 10 amino acids, and carbohydrate analysis indicates SIALP and IALP are identical to each other except in carbohydrate content, and that the SIALP is either a product of the IALP gene or a product of addition of carbohydrate including sialic acid to IALP which was taken up into the hepatocyte by endocytosis.
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