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• W1969454710 startingPage "363" @default.
• W1969454710 abstract "Fibrinogen has been modified proteolytically by a crude bacterial enzyme to produce highly ordered microcrystalline and crystalline forms (see also Tooney & Cohen, 1972; Cohen & Tooney, 1974). We present here a description of preparative methods, a survey of the electron microscope image and preliminary chemical and crystallographic data. The modified fibrinogen is largely intact and highly clottable. Many of the electron microscopic images of the modified fibrogen aggregates have a 450 Å axial repeat; a number of these ordered forms, including fibrin, can be derived from one or two basic arrays. We infer from these images that fibrinogen is 450 Å long and non-polar, i.e. that there is a 2-fold axis perpendicular to the long axis of the molecule. Filaments of fibrinogen bonded end-to-end may be a feature of all these arrays." @default.
• W1969454710 created "2016-06-24" @default.
• W1969454710 creator A5047537875 @default.
• W1969454710 creator A5070776715 @default.
• W1969454710 date "1977-02-01" @default.
• W1969454710 modified "2023-10-15" @default.
• W1969454710 title "Crystalline states of a modified fibrinogen" @default.
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• W1969454710 doi "https://doi.org/10.1016/s0022-2836(77)80077-6" @default.
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