title: Isolation, purification, and the amino acid sequence of a secretory trypsin inhibitor from the chicken pancreas.
abstract: A trypsin inhibitor is secreted in the pancreatic juice of the chick. Extracts from tissue have an inhibitor that corresponds to the secreted inhibitor on the basis of chromatography on DEAE-cellulose. The secretory inhibitor was purified by anion- and cation-exchange chromatography and by preparative isoelectric focusing. The purified inhibitor has 69 amino acids and is highly homologous with the secretory inhibitor from the turkey pancreas.
authors.affiliation: Department of Animal Sciences, Washington State University, Pullman 99164-6320.
authors.forename: M H
authors.initials: MH
authors.lastname: Pubols
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens / Q000378:metabolism*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D007525:Isoelectric Focusing; D008969:Molecular Sequence Data; D010189:Pancreatic Juice / Q000032:analysis*; D014361:Trypsin Inhibitors / Q000032:analysis / Q000302:isolation & purification*
chemical_list: D014361:Trypsin Inhibitors