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Identification of a Glu > Lys substitution in the activation segment of human pepsinogen A‐3 and ‐5 isozymogens by peptide mapping using endoproteinase Lys‐C
Author(s) -
Bank Ruud A.,
Crusius Bart C.,
Zwiers Toon,
Meuwissen Stephan G.M.,
Arwert Fre,
Pronk Jan C.
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80235-7
Subject(s) - peptide , chemistry , biochemistry , peptide sequence , pepsin , amino acid substitution , amino acid , dna , microbiology and biotechnology , mutation , stereochemistry , biology , gene , enzyme
The isozymogens PGA‐3 and PGA‐5 of human pepsinogen A were digested with endoproteinase Lys‐C. The peptides were separated by reverse‐phase HPLC. PGA‐5 showed a peak strongly absorbing at 254 nm absent in PGA‐3. Analysis of amino acid composition using the Pico‐Tag methodology combined with DABITC‐sequencing reveals the sequence Tyr‐Phe‐Pro‐Gln‐Trp‐Lys (peptide 37–43 of the activation segment). This confirms a study at the DNA level by our group [16] suggesting a Glu > Lys mutation at position 43 in the activation segment of PGA‐5. Furthermore, it is proposed that the number of genetic variants of PGA is higher than is actually seen by electrophoresis.