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本文引用的文献

1
Collagen from common minke whale (Balaenoptera acutorostrata) unesu.来自小须鲸(Balaenoptera acutorostrata)的胶原蛋白unesu。 你提供的内容似乎不太完整或存在拼写错误,“unesu”不太明确其确切含义。
Food Chem. 2008 Nov 15;111(2):296-301. doi: 10.1016/j.foodchem.2008.03.087. Epub 2008 Apr 6.
2
Isolation and characterization of collagen from the skin of deep-sea redfish (Sebastes mentella).从深海红鱼(Sebastes mentella)皮肤中分离和鉴定胶原蛋白。
J Food Sci. 2007 Oct;72(8):E450-5. doi: 10.1111/j.1750-3841.2007.00478.x.
3
Anti-inflammatory activity of emu oils in rats.鸸鹋油对大鼠的抗炎活性。
Inflammopharmacology. 1997;5(2):127-32. doi: 10.1007/s10787-997-0021-x.
4
Isolation and characterization of collagen from brown backed toadfish (Lagocephalus gloveri) skin.从褐背蟾鱼(Lagocephalus gloveri)皮肤中分离和鉴定胶原蛋白。
Bioresour Technol. 2006 Jan;97(2):191-7. doi: 10.1016/j.biortech.2005.02.024.
5
Collagen from diamondback squid (Thysanoteuthis rhombus) outer skin.来自菱鳍乌贼(Thysanoteuthis rhombus)外皮的胶原蛋白。
Z Naturforsch C J Biosci. 2004 Mar-Apr;59(3-4):271-5. doi: 10.1515/znc-2004-3-426.
6
Extraction and characterization of collagen with or without telopeptides from chicken skin.从鸡皮中提取有或无端肽的胶原蛋白并进行表征。
Poult Sci. 2003 Mar;82(3):503-9. doi: 10.1093/ps/82.3.503.
7
Marine sponge collagen: isolation, characterization and effects on the skin parameters surface-pH, moisture and sebum.海洋海绵胶原蛋白:分离、表征及其对皮肤参数表面pH值、水分和皮脂的影响。
Eur J Pharm Biopharm. 2002 Jan;53(1):107-13. doi: 10.1016/s0939-6411(01)00192-8.
8
Fish skin type I collagen: wide distribution of an alpha 3 subunit in teleosts.鱼皮I型胶原蛋白:硬骨鱼中α3亚基的广泛分布。
Comp Biochem Physiol B. 1987;88(1):27-34. doi: 10.1016/0305-0491(87)90074-5.
9
New insight into protein secondary structure from resolution-enhanced infrared spectra.从分辨率增强红外光谱中获得的蛋白质二级结构新见解。
Biochim Biophys Acta. 1988 Jan 29;952(2):115-30. doi: 10.1016/0167-4838(88)90107-0.
10
Fourier transform IR spectroscopy of collagen and gelatin solutions: deconvolution of the amide I band for conformational studies.胶原蛋白和明胶溶液的傅里叶变换红外光谱:用于构象研究的酰胺I带去卷积
Biopolymers. 1988 Nov;27(11):1749-60. doi: 10.1002/bip.360271105.

鸸鹋(Dromaius novaehollandiae)皮中胶原蛋白的特性研究。

Characterization of collagen from emu (Dromaius novaehollandiae) skins.

作者信息

Nagai Takeshi, Tanoue Yasuhiro, Kai Norihisa, Suzuki Nobutaka

机构信息

Graduate School of Agricultural Sciences, Yamagata University, Tsuruoka, Yamagata 9978555 Japan ; The United Graduate School of Agricultural Sciences, Iwate University, Morioka, Iwate 0208550 Japan ; Graduate School, Prince of Songkla University, Songkhla, 90112 Thailand.

National Fisheries University, Shimonoseki, Yamaguchi 7596595 Japan.

出版信息

J Food Sci Technol. 2015 Apr;52(4):2344-51. doi: 10.1007/s13197-014-1266-1. Epub 2014 Apr 24.

DOI:10.1007/s13197-014-1266-1
PMID:25829618
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4375231/
Abstract

Collagen from emu skins as a by-product was prepared. The skins were hardly solubilized in acetic acid, however were successfully solubilized on digestion with 10 % pepsin (w/w) for 4 days. The yield of pepsin-solubilized collagen (PSC) was about 27.3 %, on a raw weight basis. By SDS-PAGE and CM-Toyopearl 650 M column chromatography, the presence of a fourth subunit that was previously designated α4 was confirmed. The denaturation temperature of the PSC was 31.5 °C, about 6-7 °C lower than that from the porcine skins. ATR-FTIR analysis indicated that the helical arrangements of the PSC from emu skins existed and its structures of PSC were changed slightly due to the loss of N- and C-terminus domains in similar to that from the porcine skins. That is, the PSC from emu skins did not possess telopeptide chains as major portion of antigenic sites in collagen. The present study indicates that a large quantity of emu skins as by-products have potential as a good alternative source of high-quality collagen for industrial purposes in the foods, cosmetics, and pharmaceutical and biomedical fields.

摘要

制备了来自鸸鹋皮的胶原蛋白作为副产品。这些皮在乙酸中几乎不溶解,然而在用10%(w/w)胃蛋白酶消化4天后成功溶解。以原始重量计算,胃蛋白酶溶解胶原蛋白(PSC)的产率约为27.3%。通过SDS-PAGE和CM-Toyopearl 650M柱色谱法,证实了先前命名为α4的第四个亚基的存在。PSC的变性温度为31.5℃,比猪皮中的低约6-7℃。ATR-FTIR分析表明,鸸鹋皮PSC存在螺旋结构,并且由于N端和C端结构域的缺失,其结构与猪皮中的类似,略有变化。也就是说,鸸鹋皮PSC不具有作为胶原蛋白中主要抗原位点的端肽链。本研究表明,大量作为副产品的鸸鹋皮有潜力成为食品、化妆品、制药和生物医学领域工业用途中优质胶原蛋白的良好替代来源。