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ELSEVIER Journal of Chromatography B, 688 (1997) 213-220
JOURNALOF
CHROMATOGRAPHY B
Fast detection of phosphorylation of human pepsinogen A, human
pepsinogen C and swine pepsinogen using a combination of
reversed-phase high-performance liquid chromatography and
capillary zone electrophoresis for peptide mapping
Radovan Hynek"'*, Vficlav Kagi~kab,Zdenka Kurerovfi c, Jan K~g a
aDepartment of Biochemistry and Microbiology, Institute of Chemical Technology, Technichi 5 166 28 Prague 6, Czech Republic
hlnstitute of Organic Chemistry and Biochemistry, Czech Academy of Sciences, Flemingovo nfm. 2 166 10 Prague 6, Czech Republic
~Department of Pathological Physiology, 1st Faculty of Medicine, Charles University, U nemocnice 5 128 53 Prague 2,
Czech Republic
Received 15 April 1996; revised 11 June 1996; accepted 24 June 1996
Abstract
A combination of reversed-phase high-performance liquid chromatography (RP-HPLC) and capillary zone electrophoresis
(CZE) was used for characterization of a-chymotryptic digests of human pepsinogen A, human pepsinogen C (both isolated
from stomach mucosa of patients suffering from gastric cancer), swine pepsinogen and their dephosphorylated forms.
Combining RP-HPLC and CZE for peptide mapping allowed to detect phosphorylations in molecules of the above
mentioned gastric zymogens. We have found one phosphate group in the molecule of human pepsinogen A and two
phosphate groups in the molecule of human pepsinogen C. The investigated sample was obtained from stomach mucosa of a
patient suffering from gastric cancer. An increased number of phosphate groups in molecules of human pepsinogen seems to
be associated with gastric cancer. The developed method represent a suitable tool for studying relationships between specific
phosphorylations of proteins and cancerogenesis or potentially could serve for early diagnosis of gastric cancer.
Keywords: Peptide mapping; Phosphorylation
COMPOUND INDEX:
Pepsinogens
1. Introduction
Pepsinogens are produced in stomach mucosa cells
Corresponding author
as prepepsinogens with an N-terminal signal se-
quence [1], which serves for transport across the
endoplasmatic reticulum. Pepsinogen consists of a
single polypeptide chain with an average relative
molecular mass of 42 000. Its catalytic site contains
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