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Chain pairs in the crosslinking of fibrin
Authors:L Lorand  D Chenoweth  R A Domanik
Affiliation:1. Department of Energy Systems Research, Ajou University, Suwon, 16499, South Korea;2. Department of Biomedical Engineering & Department of Electronic Engineering, Hanyang University, Seoul, 04763, South Korea;1. Armor, 7 rue de la Pélissière, 44118, La Chevrolière, France;2. Institut des Matériaux Jean Rouxel (IMN), CNRS UMR 6502 Université de Nantes, 44322, Nantes, Cedex 3, France;1. Department of Biotechnology, Dr. Babasaheb Ambedkar Marathwada University, Sub Campus Osmanabad, 413501, Maharashtra, India;2. BioEra Life Sciences Pvt. Ltd., Survey Number 125, Mumbai - Bangalore Highway, Tathawade, Pune, 411033, Maharashtra, India;3. School of Pharmaceutical Sciences, Zhejiang Chinese Medical University, Hangzhou, Zhejiang, 310053, PR China;4. Laboratory of Applied Microbiology, School of Life Sciences, Jawaharlal Nehru University, New Delhi, 110067, India;1. Dalian Ocean University, Dalian 116023, China;2. Key Laboratory of Environment Controlled Aquaculture, Ministry of Education, Dalian 116023, China;3. Liaoning Normal University, Dalian 116081, China;4. College of Life Science, Dalian 116081, China;5. School of Marine Sciences, Ningbo University, Ningbo 315211, China
Abstract:After sultifolysis, enzymatically crosslinked fibrin yields fragments which are different from those obtainable from non-crosslinked material. The α and γ chains of the latter disappear almost entirely and crosslinking bands appear which move slower in electrophoresis. Prominent among these is one with the mobility calculated for an α-γ hybrid chain dimeric combination. The β chain of fibrin appears to be unaffected by crosslinking.
Keywords:
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