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Volumn 64, Issue 14, 2016, Pages 2962-2970

Efficient Absorption of X-Hydroxyproline (Hyp)-Gly after Oral Administration of a Novel Gelatin Hydrolysate Prepared Using Ginger Protease

Author keywords

absorption; collagen; gelatin hydrolysate; ginger; hydroxyproline; LC MS

Indexed keywords

ABSORPTION; AMINO ACIDS; BLOOD; COLLAGEN; FOOD ADDITIVES; PEPTIDES;

EID: 84964577883     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/acs.jafc.6b00609     Document Type: Article
Times cited : (48)

References (44)
  • 1
    • 0015624009 scopus 로고
    • The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen
    • Berg, R. A.; Prockop, D. J. The thermal transition of a non-hydroxylated form of collagen. Evidence for a role for hydroxyproline in stabilizing the triple-helix of collagen Biochem. Biophys. Res. Commun. 1973, 52, 115-120 10.1016/0006-291X(73)90961-3
    • (1973) Biochem. Biophys. Res. Commun. , vol.52 , pp. 115-120
    • Berg, R.A.1    Prockop, D.J.2
  • 3
    • 84860342238 scopus 로고    scopus 로고
    • Effect of the novel low molecular weight hydrolyzed chicken sternal cartilage extract, BioCell Collagen, on improving osteoarthritis-related symptoms: A randomized, double-blind, placebo-controlled trial
    • Schauss, A. G.; Stenehjem, J.; Park, J.; Endres, J. R.; Clewell, A. Effect of the novel low molecular weight hydrolyzed chicken sternal cartilage extract, BioCell Collagen, on improving osteoarthritis-related symptoms: a randomized, double-blind, placebo-controlled trial J. Agric. Food Chem. 2012, 60, 4096-4101 10.1021/jf205295u
    • (2012) J. Agric. Food Chem. , vol.60 , pp. 4096-4101
    • Schauss, A.G.1    Stenehjem, J.2    Park, J.3    Endres, J.R.4    Clewell, A.5
  • 4
    • 8744293542 scopus 로고    scopus 로고
    • Assessment of effectiveness of oral administration of collagen peptide on bone metabolism in growing and mature rats
    • Wu, J.; Fujioka, M.; Sugimoto, K.; Mu, G.; Ishimi, Y. Assessment of effectiveness of oral administration of collagen peptide on bone metabolism in growing and mature rats J. Bone Miner. Metab. 2004, 22, 547-553 10.1007/s00774-004-0522-2
    • (2004) J. Bone Miner. Metab. , vol.22 , pp. 547-553
    • Wu, J.1    Fujioka, M.2    Sugimoto, K.3    Mu, G.4    Ishimi, Y.5
  • 5
    • 27944457530 scopus 로고    scopus 로고
    • Increase in bone mineral density through oral administration of shark gelatin to ovariectomized rats
    • Nomura, Y.; Oohashi, K.; Watanabe, M.; Kasugai, S. Increase in bone mineral density through oral administration of shark gelatin to ovariectomized rats Nutrition 2005, 21, 1120-1126 10.1016/j.nut.2005.03.007
    • (2005) Nutrition , vol.21 , pp. 1120-1126
    • Nomura, Y.1    Oohashi, K.2    Watanabe, M.3    Kasugai, S.4
  • 7
    • 65249112736 scopus 로고    scopus 로고
    • Antihypertensive effects and endothelial progenitor cell activation by intake of chicken collagen hydrolysate in pre- and mild-hypertension
    • Saiga-Egusa, A.; Iwai, K.; Hayakawa, T.; Takahata, Y.; Morimatsu, F. Antihypertensive effects and endothelial progenitor cell activation by intake of chicken collagen hydrolysate in pre- and mild-hypertension Biosci., Biotechnol., Biochem. 2009, 73, 422-424 10.1271/bbb.80189
    • (2009) Biosci., Biotechnol., Biochem. , vol.73 , pp. 422-424
    • Saiga-Egusa, A.1    Iwai, K.2    Hayakawa, T.3    Takahata, Y.4    Morimatsu, F.5
  • 8
    • 84926315093 scopus 로고    scopus 로고
    • Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats
    • Huang, S. L.; Hung, C. C.; Jao, C. L.; Tung, Y. S.; Hsu, K. C. Porcine skin gelatin hydrolysate as a dipeptidyl peptidase IV inhibitor improves glycemic control in streptozotocin-induced diabetic rats J. Funct. Foods 2014, 11, 235-242 10.1016/j.jff.2014.09.010
    • (2014) J. Funct. Foods , vol.11 , pp. 235-242
    • Huang, S.L.1    Hung, C.C.2    Jao, C.L.3    Tung, Y.S.4    Hsu, K.C.5
  • 9
    • 84931025549 scopus 로고    scopus 로고
    • Improvement of glycemic control in streptozotocin-induced diabetic rats by Atlantic salmon skin gelatin hydrolysate as the dipeptidyl-peptidase IV inhibitor
    • Hsieh, C. H.; Wang, T. Y.; Hung, C. C.; Chen, M. C.; Hsu, K. C. Improvement of glycemic control in streptozotocin-induced diabetic rats by Atlantic salmon skin gelatin hydrolysate as the dipeptidyl-peptidase IV inhibitor Food Funct. 2015, 6, 1887-1892 10.1039/C5FO00124B
    • (2015) Food Funct. , vol.6 , pp. 1887-1892
    • Hsieh, C.H.1    Wang, T.Y.2    Hung, C.C.3    Chen, M.C.4    Hsu, K.C.5
  • 10
    • 79961026637 scopus 로고    scopus 로고
    • Functional and bioactive properties of collagen and gelatin from alternative sources: A review
    • Gómez-Guillén, M. C.; Giménez, B.; López-Caballero, M. E.; Montero, M. P. Functional and bioactive properties of collagen and gelatin from alternative sources: a review Food Hydrocolloids 2011, 25, 1813-1827 10.1016/j.foodhyd.2011.02.007
    • (2011) Food Hydrocolloids , vol.25 , pp. 1813-1827
    • Gómez-Guillén, M.C.1    Giménez, B.2    López-Caballero, M.E.3    Montero, M.P.4
  • 11
    • 0041977278 scopus 로고    scopus 로고
    • Production of tripeptide from gelatin using collagenase-immobilized porous hollow-fiber membrane
    • Fujita, A.; Kawakita, H.; Saito, K.; Sugita, K.; Tamada, M.; Sugo, T. Production of tripeptide from gelatin using collagenase-immobilized porous hollow-fiber membrane Biotechnol. Prog. 2003, 19, 1365-1367 10.1021/bp030004i
    • (2003) Biotechnol. Prog. , vol.19 , pp. 1365-1367
    • Fujita, A.1    Kawakita, H.2    Saito, K.3    Sugita, K.4    Tamada, M.5    Sugo, T.6
  • 12
    • 84913603842 scopus 로고    scopus 로고
    • Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity
    • Hatanaka, T.; Kawakami, K.; Uraji, M. Inhibitory effect of collagen-derived tripeptides on dipeptidylpeptidase-IV activity J. Enzyme Inhib. Med. Chem. 2014, 29, 823-828 10.3109/14756366.2013.858143
    • (2014) J. Enzyme Inhib. Med. Chem. , vol.29 , pp. 823-828
    • Hatanaka, T.1    Kawakami, K.2    Uraji, M.3
  • 13
    • 0034840775 scopus 로고    scopus 로고
    • Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate
    • Kim, S. K.; Byun, H. G.; Park, P. J.; Shahidi, F. Angiotensin I converting enzyme inhibitory peptides purified from bovine skin gelatin hydrolysate J. Agric. Food Chem. 2001, 49, 2992-2997 10.1021/jf001119u
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2992-2997
    • Kim, S.K.1    Byun, H.G.2    Park, P.J.3    Shahidi, F.4
  • 14
    • 0034951098 scopus 로고    scopus 로고
    • Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin
    • Byun, H. G.; Kim, S. K. Purification and characterization of angiotensin I converting enzyme (ACE) inhibitory peptides from Alaska pollack (Theragra chalcogramma) skin Process Biochem. 2001, 36, 1155-1162 10.1016/S0032-9592(00)00297-1
    • (2001) Process Biochem. , vol.36 , pp. 1155-1162
    • Byun, H.G.1    Kim, S.K.2
  • 15
    • 0031148006 scopus 로고    scopus 로고
    • In vitro and in vivo anti-platelet effects of enzymatic hydrolysates of collagen and collagen-related peptides
    • Nonaka, I.; Katsuda, S.; Ohmori, T.; Shigehisa, T.; Nakagami, T.; Maruyama, S. In vitro and in vivo anti-platelet effects of enzymatic hydrolysates of collagen and collagen-related peptides Biosci., Biotechnol., Biochem. 1997, 61, 772-775 10.1271/bbb.61.772
    • (1997) Biosci., Biotechnol., Biochem. , vol.61 , pp. 772-775
    • Nonaka, I.1    Katsuda, S.2    Ohmori, T.3    Shigehisa, T.4    Nakagami, T.5    Maruyama, S.6
  • 16
    • 0001638603 scopus 로고
    • Gastrointestinal absorption and renal excretion of hydroxyproline peptides
    • Prockop, D. J.; Keiser, H. R.; Sjoerdsma, A. Gastrointestinal absorption and renal excretion of hydroxyproline peptides Lancet 1962, 280, 527-528 10.1016/S0140-6736(62)90400-2
    • (1962) Lancet , vol.280 , pp. 527-528
    • Prockop, D.J.1    Keiser, H.R.2    Sjoerdsma, A.3
  • 18
    • 34249852152 scopus 로고    scopus 로고
    • Comparison of quantity and structures of hydroxyproline-containing peptides in human blood after oral ingestion of gelatin hydrolysates from different sources
    • Ohara, H.; Matsumoto, H.; Ito, K.; Iwai, K.; Sato, K. Comparison of quantity and structures of hydroxyproline-containing peptides in human blood after oral ingestion of gelatin hydrolysates from different sources J. Agric. Food Chem. 2007, 55, 1532-1535 10.1021/jf062834s
    • (2007) J. Agric. Food Chem. , vol.55 , pp. 1532-1535
    • Ohara, H.1    Matsumoto, H.2    Ito, K.3    Iwai, K.4    Sato, K.5
  • 19
    • 79960155800 scopus 로고    scopus 로고
    • Identification of a novel food-derived collagen peptide, hydroxyprolyl-glycine, in human peripheral blood by pre-column derivatisation with phenyl isothiocyanate
    • Shigemura, Y.; Akaba, S.; Kawashima, E.; Park, E. Y.; Nakamura, Y.; Sato, K. Identification of a novel food-derived collagen peptide, hydroxyprolyl-glycine, in human peripheral blood by pre-column derivatisation with phenyl isothiocyanate Food Chem. 2011, 129, 1019-1024 10.1016/j.foodchem.2011.05.066
    • (2011) Food Chem. , vol.129 , pp. 1019-1024
    • Shigemura, Y.1    Akaba, S.2    Kawashima, E.3    Park, E.Y.4    Nakamura, Y.5    Sato, K.6
  • 20
    • 34447579220 scopus 로고    scopus 로고
    • Transport of a tripeptide, Gly-Pro-Hyp, across the porcine intestinal brush-border membrane
    • Aito-Inoue, M.; Lackeyram, D.; Fan, M. Z.; Sato, K.; Mine, Y. Transport of a tripeptide, Gly-Pro-Hyp, across the porcine intestinal brush-border membrane J. Pept. Sci. 2007, 13, 468-474 10.1002/psc.870
    • (2007) J. Pept. Sci. , vol.13 , pp. 468-474
    • Aito-Inoue, M.1    Lackeyram, D.2    Fan, M.Z.3    Sato, K.4    Mine, Y.5
  • 21
    • 69949118070 scopus 로고    scopus 로고
    • Absorption of hydroxyproline-containing peptides in vascularly perfused rat small intestine in situ
    • Liu, C.; Sugita, K.; Nihei, K.; Yoneyama, K.; Tanaka, H. Absorption of hydroxyproline-containing peptides in vascularly perfused rat small intestine in situ Biosci., Biotechnol., Biochem. 2009, 73, 1741-1747 10.1271/bbb.90050
    • (2009) Biosci., Biotechnol., Biochem. , vol.73 , pp. 1741-1747
    • Liu, C.1    Sugita, K.2    Nihei, K.3    Yoneyama, K.4    Tanaka, H.5
  • 23
    • 59849104535 scopus 로고    scopus 로고
    • Effect of prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin
    • Shigemura, Y.; Iwai, K.; Morimatsu, F.; Iwamoto, T.; Mori, T.; Oda, C.; Taira, T.; Park, E. Y.; Nakamura, Y.; Sato, K. Effect of prolyl-hydroxyproline (Pro-Hyp), a food-derived collagen peptide in human blood, on growth of fibroblasts from mouse skin J. Agric. Food Chem. 2009, 57, 444-449 10.1021/jf802785h
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 444-449
    • Shigemura, Y.1    Iwai, K.2    Morimatsu, F.3    Iwamoto, T.4    Mori, T.5    Oda, C.6    Taira, T.7    Park, E.Y.8    Nakamura, Y.9    Sato, K.10
  • 24
    • 77950236472 scopus 로고    scopus 로고
    • Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts
    • Ohara, H.; Ichikawa, S.; Matsumoto, H.; Akiyama, M.; Fujimoto, N.; Kobayashi, T.; Tajima, S. Collagen-derived dipeptide, proline-hydroxyproline, stimulates cell proliferation and hyaluronic acid synthesis in cultured human dermal fibroblasts J. Dermatol. 2010, 37, 330-338 10.1111/j.1346-8138.2010.00827.x
    • (2010) J. Dermatol. , vol.37 , pp. 330-338
    • Ohara, H.1    Ichikawa, S.2    Matsumoto, H.3    Akiyama, M.4    Fujimoto, N.5    Kobayashi, T.6    Tajima, S.7
  • 25
    • 84919930729 scopus 로고    scopus 로고
    • Oral collagen-derived dipeptides, prolyl-hydroxyproline and hydroxyprolyl-glycine, ameliorate skin barrier dysfunction and alter gene expression profiles in the skin
    • Shimizu, J.; Asami, N.; Kataoka, A.; Sugihara, F.; Inoue, N.; Kimira, Y.; Wada, M.; Mano, H. Oral collagen-derived dipeptides, prolyl-hydroxyproline and hydroxyprolyl-glycine, ameliorate skin barrier dysfunction and alter gene expression profiles in the skin Biochem. Biophys. Res. Commun. 2015, 456, 626-630 10.1016/j.bbrc.2014.12.006
    • (2015) Biochem. Biophys. Res. Commun. , vol.456 , pp. 626-630
    • Shimizu, J.1    Asami, N.2    Kataoka, A.3    Sugihara, F.4    Inoue, N.5    Kimira, Y.6    Wada, M.7    Mano, H.8
  • 26
    • 84918507596 scopus 로고    scopus 로고
    • Highly accurate quantification of hydroxyproline-containing peptides in blood using a protease digest of stable isotope-labeled collagen
    • Taga, Y.; Kusubata, M.; Ogawa-Goto, K.; Hattori, S. Highly accurate quantification of hydroxyproline-containing peptides in blood using a protease digest of stable isotope-labeled collagen J. Agric. Food Chem. 2014, 62, 12096-12102 10.1021/jf5039597
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 12096-12102
    • Taga, Y.1    Kusubata, M.2    Ogawa-Goto, K.3    Hattori, S.4
  • 27
    • 0022655977 scopus 로고
    • Chemotactic activity of collagen-like polypeptides for human peripheral blood neutrophils
    • Laskin, D. L.; Kimura, T.; Sakakibara, S.; Riley, D. J.; Berg, R. A. Chemotactic activity of collagen-like polypeptides for human peripheral blood neutrophils J. Leukocyte Biol. 1986, 39, 255-266
    • (1986) J. Leukocyte Biol. , vol.39 , pp. 255-266
    • Laskin, D.L.1    Kimura, T.2    Sakakibara, S.3    Riley, D.J.4    Berg, R.A.5
  • 28
    • 69949177556 scopus 로고    scopus 로고
    • Blood concentration of food-derived peptides following oral intake of chicken collagen hydrolysate and its angiotensin-converting enzyme inhibitory activity in healthy volunteers
    • Iwai, K.; Zhang, Y.; Kouguchi, T.; Saiga-Egusa, A.; Shimizu, M.; Ohmori, T.; Takahata, Y.; Morimatsu, F. Blood concentration of food-derived peptides following oral intake of chicken collagen hydrolysate and its angiotensin-converting enzyme inhibitory activity in healthy volunteers Nippon Shokuhin Kagaku Kogaku Kaishi 2009, 56, 326-330 10.3136/nskkk.56.326
    • (2009) Nippon Shokuhin Kagaku Kogaku Kaishi , vol.56 , pp. 326-330
    • Iwai, K.1    Zhang, Y.2    Kouguchi, T.3    Saiga-Egusa, A.4    Shimizu, M.5    Ohmori, T.6    Takahata, Y.7    Morimatsu, F.8
  • 29
  • 30
    • 0028896997 scopus 로고
    • Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing
    • Ohtsuki, K.; Taguchi, K.; Sato, K.; Kawabata, M. Purification of ginger proteases by DEAE-Sepharose and isoelectric focusing Biochim. Biophys. Acta, Gen. Subj. 1995, 1243, 181-184 10.1016/0304-4165(94)00145-N
    • (1995) Biochim. Biophys. Acta, Gen. Subj. , vol.1243 , pp. 181-184
    • Ohtsuki, K.1    Taguchi, K.2    Sato, K.3    Kawabata, M.4
  • 31
    • 0034015436 scopus 로고    scopus 로고
    • Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale
    • Choi, K. H.; Laursen, R. A. Amino-acid sequence and glycan structures of cysteine proteases with proline specificity from ginger rhizome Zingiber officinale Eur. J. Biochem. 2000, 267, 1516-1526 10.1046/j.1432-1327.2000.01152.x
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1516-1526
    • Choi, K.H.1    Laursen, R.A.2
  • 32
    • 84987368845 scopus 로고
    • Ginger rhizome: A new source of proteolytic enzyme
    • Thompson, E. H.; Wolf, I. D.; Allen, C. E. Ginger rhizome: a new source of proteolytic enzyme J. Food Sci. 1973, 38, 652-655 10.1111/j.1365-2621.1973.tb02836.x
    • (1973) J. Food Sci. , vol.38 , pp. 652-655
    • Thompson, E.H.1    Wolf, I.D.2    Allen, C.E.3
  • 34
    • 35448933148 scopus 로고    scopus 로고
    • Plant collagenase: Unique collagenolytic activity of cysteine proteases from ginger
    • Kim, M.; Hamilton, S. E.; Guddat, L. W.; Overall, C. M. Plant collagenase: unique collagenolytic activity of cysteine proteases from ginger Biochim. Biophys. Acta, Gen. Subj. 2007, 1770, 1627-1635 10.1016/j.bbagen.2007.08.003
    • (2007) Biochim. Biophys. Acta, Gen. Subj. , vol.1770 , pp. 1627-1635
    • Kim, M.1    Hamilton, S.E.2    Guddat, L.W.3    Overall, C.M.4
  • 35
    • 9644275379 scopus 로고    scopus 로고
    • Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (ginger rhizome)
    • Naveena, B. M.; Mendiratta, S. K.; Anjaneyulu, A. S. Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (ginger rhizome) Meat Sci. 2004, 68, 363-369 10.1016/j.meatsci.2004.04.004
    • (2004) Meat Sci. , vol.68 , pp. 363-369
    • Naveena, B.M.1    Mendiratta, S.K.2    Anjaneyulu, A.S.3
  • 36
    • 84860375419 scopus 로고    scopus 로고
    • Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins
    • Ha, M.; Bekhit, A. E. D.; Carne, A.; Hopkins, D. L. Characterisation of commercial papain, bromelain, actinidin and zingibain protease preparations and their activities toward meat proteins Food Chem. 2012, 134, 95-105 10.1016/j.foodchem.2012.02.071
    • (2012) Food Chem. , vol.134 , pp. 95-105
    • Ha, M.1    Bekhit, A.E.D.2    Carne, A.3    Hopkins, D.L.4
  • 37
    • 65649105394 scopus 로고    scopus 로고
    • Characterization of ginger proteases and their potential as a rennin replacement
    • Su, H. P.; Huang, M. J.; Wang, H. T. Characterization of ginger proteases and their potential as a rennin replacement J. Sci. Food Agric. 2009, 89, 1178-1185 10.1002/jsfa.3572
    • (2009) J. Sci. Food Agric. , vol.89 , pp. 1178-1185
    • Su, H.P.1    Huang, M.J.2    Wang, H.T.3
  • 38
    • 79952900207 scopus 로고    scopus 로고
    • Ginger rhizome as a potential source of milk coagulating cysteine protease
    • Hashim, M. M.; Mingsheng, D.; Iqbal, M. F.; Xiaohong, C. Ginger rhizome as a potential source of milk coagulating cysteine protease Phytochemistry 2011, 72, 458-464 10.1016/j.phytochem.2010.12.002
    • (2011) Phytochemistry , vol.72 , pp. 458-464
    • Hashim, M.M.1    Mingsheng, D.2    Iqbal, M.F.3    Xiaohong, C.4
  • 39
    • 0033533253 scopus 로고    scopus 로고
    • The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale
    • Choi, K. H.; Laursen, R. A.; Allen, K. N. The 2.1 A structure of a cysteine protease with proline specificity from ginger rhizome, Zingiber officinale Biochemistry 1999, 38, 11624-11633 10.1021/bi990651b
    • (1999) Biochemistry , vol.38 , pp. 11624-11633
    • Choi, K.H.1    Laursen, R.A.2    Allen, K.N.3
  • 40
    • 84905387556 scopus 로고    scopus 로고
    • Stable isotope-labeled collagen: A novel and versatile tool for quantitative collagen analyses using mass spectrometry
    • Taga, Y.; Kusubata, M.; Ogawa-Goto, K.; Hattori, S. Stable isotope-labeled collagen: a novel and versatile tool for quantitative collagen analyses using mass spectrometry J. Proteome Res. 2014, 13, 3671-3678 10.1021/pr500213a
    • (2014) J. Proteome Res. , vol.13 , pp. 3671-3678
    • Taga, Y.1    Kusubata, M.2    Ogawa-Goto, K.3    Hattori, S.4
  • 41
    • 84954183494 scopus 로고    scopus 로고
    • Developmental stage-dependent regulation of prolyl 3-hydroxylation in tendon type I collagen
    • Taga, Y.; Kusubata, M.; Ogawa-Goto, K.; Hattori, S. Developmental stage-dependent regulation of prolyl 3-hydroxylation in tendon type I collagen J. Biol. Chem. 2016, 291, 837-847 10.1074/jbc.M115.686105
    • (2016) J. Biol. Chem. , vol.291 , pp. 837-847
    • Taga, Y.1    Kusubata, M.2    Ogawa-Goto, K.3    Hattori, S.4
  • 42
    • 84964674316 scopus 로고    scopus 로고
    • Influence on quantity of hydroxyproline-containing peptides in human blood after oral ingestion by the different average molecular weight collagen peptides
    • Ichikawa, S.; Ohara, H.; Ito, K.; Oba, C.; Matsumoto, H.; Takeuchi, Y.; Kanegae, M. Influence on quantity of hydroxyproline-containing peptides in human blood after oral ingestion by the different average molecular weight collagen peptides Jpn. J. Med. Pharm. Sci. 2009, 62, 801-807
    • (2009) Jpn. J. Med. Pharm. Sci. , vol.62 , pp. 801-807
    • Ichikawa, S.1    Ohara, H.2    Ito, K.3    Oba, C.4    Matsumoto, H.5    Takeuchi, Y.6    Kanegae, M.7
  • 43
    • 84946902117 scopus 로고    scopus 로고
    • Absorption and plasma kinetics of collagen tripeptide after peroral or intraperitoneal administration in rats
    • Yamamoto, S.; Hayasaka, F.; Deguchi, K.; Okudera, T.; Furusawa, T.; Sakai, Y. Absorption and plasma kinetics of collagen tripeptide after peroral or intraperitoneal administration in rats Biosci., Biotechnol., Biochem. 2015, 79, 2026-2033 10.1080/09168451.2015.1062711
    • (2015) Biosci., Biotechnol., Biochem. , vol.79 , pp. 2026-2033
    • Yamamoto, S.1    Hayasaka, F.2    Deguchi, K.3    Okudera, T.4    Furusawa, T.5    Sakai, Y.6
  • 44
    • 0020360698 scopus 로고
    • Isolation and characterization of dipeptidyl peptidase IV from human placenta
    • Puschel, G.; Mentlein, R.; Heymann, E. Isolation and characterization of dipeptidyl peptidase IV from human placenta Eur. J. Biochem. 1982, 126, 359-365 10.1111/j.1432-1033.1982.tb06788.x
    • (1982) Eur. J. Biochem. , vol.126 , pp. 359-365
    • Puschel, G.1    Mentlein, R.2    Heymann, E.3


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