Improved chromatographic purification of human and bovine type V collagen sub-molecular species and their subunit chains from conventional crude preparations Application to cell-substratum adhesion assay for human umbilical vien endothelial cell |
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| Institution: | 1. Department of Agricultural, Food & Nutritional Science, University of Alberta, Edmonton, AB, Canada;2. Cardiovascular Research Centre, University of Alberta, Edmonton, AB, Canada;3. College of Bioscience and Biotechnology, Hunan Agricultural University, Changsha 410128, China;4. Key Laboratory of Agro-ecological Processes in Subtropical Region, Institute of Subtropical Agriculture, Chinese Academy of Sciences, Changsha, 410125, Hunan, China;1. Telethon Institute of Genetics and Medicine (TIGEM), Via dei Campi Flegrei 34, 80078 Pozzuoli, Napoli, Italy;2. Medical Genetics Unit, Department of Medical and Translational Science, Federico II University, Via Pansini 5, 80131 Napoli, Italy |
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| Abstract: | Two human type V collagen sub-molecular species, designated α1(V)]2α2(V) and α1(V)α2(V)α3(V), were purified chromatographically from a commercially available preparation, in which cystine-rich collagenous contaminants were contained, with a column packed with Fractogel EMD SO3−. From bovine crude preparations, the α1(V)]2α2(V) form free from the collagenous contaminants was purified. Type V collagen subunit chains were isolated from each type V collagen molecule by anion-exchange HPLC with a Bakerbond PEI Scout column. The highly purified human type V collagen molecules and their subunit chains were used to examine the inhibitory effect on human umbilical vein endothelial cell proliferation. It was confirmed that the α1(V) chain has inhibitory activity and it was found that the inhibitory effect of the α1(V)]2α2(V) form is stronger than that of the α1(V)α2(V)α3(V) form and that the α3(V) chain has no inhibitory activity. |
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