Analysis in gingival crevicular fluid of two oligopeptides derived from human hemoglobin beta-chain

HPLC on a reversed phase column, amino acid sequencing and mass spectrometry were used to determine the structure of two human gingival crevicular exudate oligopeptides (Leu-Thr-Pro-Glu-Glu-Lys-Ser-Ala-Val-Thr-Ala-Leu and Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe) which were shown to have been derived...

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Bibliographic Details
Published inJournal of periodontal research Vol. 31; no. 1; p. 43
Main Authors Mäkinen, K K, Sewon, L, Mäkinen, P l
Format Journal Article
LanguageEnglish
Published United States 01.01.1996
Subjects
Adult
Aged
Amino Acid Sequence
Chromatography, High Pressure Liquid
Electrophoresis, Polyacrylamide Gel
Female
Gingival Crevicular Fluid - chemistry
Gingival Crevicular Fluid - enzymology
Hemoglobins - chemistry
Hemoglobins - metabolism
Humans
Male
Middle Aged
Molecular Sequence Data
Molecular Weight
Oligopeptides - analysis
Oligopeptides - chemistry
Peptide Hydrolases - metabolism
Periodontal Diseases - metabolism
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Summary:HPLC on a reversed phase column, amino acid sequencing and mass spectrometry were used to determine the structure of two human gingival crevicular exudate oligopeptides (Leu-Thr-Pro-Glu-Glu-Lys-Ser-Ala-Val-Thr-Ala-Leu and Leu-Val-Val-Tyr-Pro-Trp-Thr-Gln-Arg-Phe) which were shown to have been derived from the beta-chain of hemoglobin. These sequences may simply represent two degradation products of the beta-chain. However, their preservation in an exudate characterized by active peptidolysis may also prompt the question about their possible more specific role.
ISSN:0022-3484
DOI:10.1111/j.1600-0765.1996.tb00462.x