Identification of a novel food-derived collagen peptide,hydroxyprolyl-glycine,in human peripheral blood by pre-column derivatisation with phenyl isothiocyanate |
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Authors: | Yasutaka Shigemura Saeko Akaba Eriko Kawashima Eun Young Park Yasushi Nakamura Kenji Sato |
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Affiliation: | 1. Osaka Yuhigaoka Gakuen Junior College, 7-72 Ikutamadera-cho, Tennoji, Osaka 543-0073, Japan;2. Division of Applied Life Sciences, Graduate School of Life and Environment Sciences, Kyoto Prefectural University, 1-5 Shimogamo, Kyoto 606-8522, Japan;3. Yokohama Research Center, Chisso Corporation, 5-1, Okawa, Kanazawa-ku, Yokohama 236-8605, Japan |
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Abstract: | Peptides in the blood of subjects before and after collagen hydrolysate ingestion were fractionated by ion exchange and size-exclusion chromatographies and then derivatised with phenyl isothiocyanate. The derivatives were characterised by reserved phase (RP)-HPLC. Prolyl-hydroxyproline (Pro-Hyp), which has been identified in the previous studies, was detected as a major food-derived collagen peptide in the blood of all subjects (n = 5). Another major peptide was identified as hydroxyprolyl-glycine (Hyp-Gly) in the blood of four subjects, which has not been detected in previous studies. The ratio of Hyp-Gly to Pro-Hyp depended on subjects and ranged from 0.00 to 5.04. Hyp-Gly was less susceptible to human serum peptidase than Pro-Hyp. Hyp-Gly enhanced the growth of mouse primary fibroblasts on collagen gels in a higher extent than Pro-Hyp. These findings suggest that Hyp-Gly plays a significant role in exerting the biological effects by ingestion of collagen hydrolysate. |
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Keywords: | Collagen Collagen hydrolysate Peptide Hyp-Gly Pro-Hyp Hyp Skin Plasma Fibroblasts |
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