Collagen fractionation: Separation of native types I, II and III by differential prectipitation☆
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2019, Materials Today AdvancesCitation Excerpt :After mincing, collagen was extracted by pepsin digestion, 1 mg/mL in 100 mM acetic acid adjusted to pH 2.5 with hydrochloric acid (HCl) [14,17]. After 24 h, the soluble collagen was separated by centrifugation and purified by sodium chloride (NaCl) fractionation at pH 2.5 and 7.4 [14,18] without separating type III collagen. The collagen precipitate at pH 7.4 was dialyzed extensively against 20 mM acetic acid.
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2018, MaterialiaCitation Excerpt :The supernatant was recovered and denatured by incubating the collagen at 30 °C for 30 min. ASC from hoki skin was prepared using salt precipitation [33]. In brief, skins were left to swell in 0.5 M acetic acid for 3 days and homogenized.
Collagen-based layer-by-layer coating on electrospun polymer scaffolds
2012, BiomaterialsCitation Excerpt :The collagen precipitate was further purified at pH 7.4 in 50 mM Tris/HCl by removal of type III collagen by precipitation with 1.7 M NaCl, followed by precipitation of type I collagen by 2.4 M NaCl. Type III collagen was further enriched by rapid (NH4)2SO4 precipitation [22]. Collagen purity was assessed by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) [23] using NuPAGE 4–12% Bis-Tris gels with MES running gel buffer (Invitrogen) at 150 V for 3 h, and using delayed reduction for type III collagen samples [24].
Type I collagen from the skin of ornate threadfin bream (Nemipterus hexodon): Characteristics and effect of pepsin hydrolysis
2011, Food ChemistryCitation Excerpt :At least 19 variants of collagen (types I–XIX) have been reported (Bailey, Paul, & Knott, 1998). Type I collagen, [α1(I)]2α2, is the major collagen found predominantly in the connective tissues, such as skin, bone, and tendon, and contains two identical α1(I) chains and one α2-chain (Trelstad, Catanese, & Rubin, 1976). Chromatographic and electrophoretic analyses revealed that most of the teleost skin collagens also contained a unique subunit, α3 (Kimura, Ohno, Miyauchi, & Uchida, 1987).
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This is publication No. 678 of the Robert W. Lovett Memorial Group for the Study of Diseases Causing Deformities. This investigation was supported by a grant from the NIH (AM 3564) and from the American Cancer Society, Massachusetts Division (No. 1441-C-1).
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Recipient Faculty Research Award, American Cancer Society (PR 107).