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 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.
Mäkinen
K K
KK
Department of Biologic and Materials Sciences, School of Dentistry, University of Michigan, Ann Arbor, USA.
Sewon
L
L
Mäkinen
P l
Pl
D000328:Adult; D000368:Aged; D000595:Amino Acid Sequence; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D005883:Gingival Crevicular Fluid / Q000737:chemistry* / Q000201:enzymology; D006454:Hemoglobins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008297:Male; D008875:Middle Aged; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009842:Oligopeptides / Q000032:analysis / Q000737:chemistry; D010447:Peptide Hydrolases / Q000378:metabolism; D010510:Periodontal Diseases / Q000378:metabolism*
D006454:Hemoglobins; D009842:Oligopeptides; D010447:Peptide Hydrolases