References
- Choe JS, Youn JY (2005) The chemical composition of barley and wheat varieties. J Korean Soc Food Sci Nutr, 34, 223-229 https://doi.org/10.3746/jkfn.2005.34.2.223
- Jun HI, Cha MN, Song GS, Yoo CS, Kim YT, Kim YS (2011) Physicochemical properties and cooking quality of naked waxy barley (Saechalssal bori). Korean J Food Preserv, 18, 165-170 https://doi.org/10.11002/kjfp.2011.18.2.165
- Park TS, Lee SY, Kim HJ, Kim KT, Kim YJ, Jeong IH, Do WN, Lee HJ (2009) Extracts of adlay, barley and rice bran have antioxidant activity and modulate fatty acid metabolism in adipocytes. Korean J Food Nutr, 22, 456-462
- McIntosh GH, Whyte J, McArthur R, Nestel PJ (1991) Barley and wheat foods: Influence on plasma cholesterol concentration in hypercholesterolemic men1-3. Am J Clin Nutr, 53, 1205-1209
- Yang EJ, Cho YS, Choi MS, Woo MN, Kim MJ, Shon MY, Lee MK (2009) Effect of young barley leaf on lipid contents and hepatic lipid-regulating enzyme activities in mice fed high-fat diet. Korean J Nutr, 42, 14-22
- Chang HG, Jung IH (1994) The physicochemical properties and cooking qualities of barley. J Korean Soc Food Nutr, 23, 816-821
- Titchenal CA, Dobbs J (2007) A system to assess the quality of food sources of calcium. J Food Compos Anal, 20, 717-724 https://doi.org/10.1016/j.jfca.2006.04.013
- Bowers GN, Brassard C (1986) Measurement of ionized calcium serum with ion-selective electrode: A mature technology that can meet the daily service needs. Clin Chem, 32, 1437-1447
- Barclay JW, Morgan A, Burgoyne RD (2005) Calciumdependent regulation of exocytosis. Cell Calcium 38, 343-353 https://doi.org/10.1016/j.ceca.2005.06.012
- Jeon SJ, Lee JH, Song KB (2010) Preparation for calcium and iron-binding peptides from rice bran protein hydrolysates. J Appl Biol Chem, 53, 174-178 https://doi.org/10.3839/jabc.2010.031
- Lee JH, Jeon SJ, Song KB (2010) Isolation of a calcium-binding fraction from hot-water extract of Smilax rhizoma. Korean J Food Preserv, 17, 903-907
- Lee SH, Song KB (2009) Isolation of a calcium-binding peptide from enzymatic hydrolysates of porcine blood plasma protein. J Korean Soc Appl Biol Chem, 52,290-294 https://doi.org/10.3839/jksabc.2009.051
- Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 https://doi.org/10.1038/227680a0
-
Ekund A (1976) On the determination of available lysine in casein and rapeseed protein concentration using 2,4,6-trinitrobenzenesulfonic acid (TNBS) as a reagent of free
$\alpha$ -amino group of lysine. Anal Chem, 70, 434-439 - Gitelman HJ (1967) An improved automated procedure for the determination of calcium in biological specimens. Anal Biochem, 18, 521-531 https://doi.org/10.1016/0003-2697(67)90110-8
- Hara H, Funabiki R, Iwata M, Yamazaki KI (1984) Portal absorption of small peptides in rats under unrestrained conditions. J Nutr, 114, 1122-1129
- Jung WK, Lee BJ, Kim SK (2006) Fish-bone peptide increases calcium solubility and bioavailability in ovariectomised rats. Brit J Nutr, 95, 124-128 https://doi.org/10.1079/BJN20051615
- Korhonen H, Pihlanto A (2006) Bioactive peptides: Production and functionality. Int Dairy J, 16, 945-960 https://doi.org/10.1016/j.idairyj.2005.10.012
- Miquel E, Alegria A, Barbera R, Farre R (2005) Speciation analysis of calcium, iron, and zinc in casein phosphopeptide fraction from toddler milk-based formula by anion exchange and reversed-phase high-performance liquid chromatography-mass spectrometry/flame atomicabsorption spectroscopy. Anal Bioanal Chem, 381, 1082-1088 https://doi.org/10.1007/s00216-004-3002-6
- Jeon SJ, Lee JH, Song KB (2010) Isolation of a calcium-binding peptide from chlorella protein hydrolysates. J Food Sci Nutr, 15, 282-286 https://doi.org/10.3746/jfn.2010.15.4.282
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