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- W2053183743 abstract "Abstract The true monomerix size of porcine aortic tropoelastin is 72,000–74,000 daltons. The newly modified isolation procedure we describe gives meterial predominantly of this molecular size with improved yields. The protein is extremely susceptible to proteolysis and steps must be taken during isolation to prevent this occurrence. The addition of di-isopropylfluorophosphate, N -ethylmaleimide, and EDTA to the initial extraction buffer has proven effective. Lower molecular weight components which are elastin-like are always isolated along with the high molecular weight material. In the absence of the inhibitors, these smaller components are greatly increased. Alanine enrichment as revealed by NH 2 -terminal analyses of the degraded material suggests that the tissue proteinases which produce these are elastase-like." @default.
- W2053183743 created "2016-06-24" @default.
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- W2053183743 date "1975-03-01" @default.
- W2053183743 modified "2023-10-05" @default.
- W2053183743 title "Tropoelastin purification: Improvements using enzyme inhibitors" @default.
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- W2053183743 doi "https://doi.org/10.1016/0003-2697(75)90425-x" @default.
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