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Collagen fibril formation in vitro. A quasielastic light-scattering study of early stages. by R.A. Gelman; K.A. Piez is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Purified rat tail tendon collagen used in our in vitro assembly studies has been characterized by quasielastic light scattering. At 4°C and neutral pH it behaves as a single monomeric species with a translational diffusion coefficient, Dzo,,,,, at infinite dilution of 0.78 X cm2/s. This value is consistent with a somewhat flexible rod (300 X 1.2 nm) having 0.5 to 1.0 g of associated water/g of protein, When the temperature of a neutral solution of this collagen (0.1 mg/ml) is raised to 26°C to initiate assembly, Dzo.ru decreases in 10 min or less to 0.15 X 10" cm2/s (Step 1) and remains constant for about 50 min (Step 2). The material present during Step 2 behaves as if it were a single high molecular weight species. These results together with earlier turbidity studies are consistent with an assembly mechanism whereby during Step 1 monomer is rapidly converted to aggregates >1500 nm long and cannot be measured, consists of lateral association of the product of Step 2 to form native fibrils. We have previously shown that in vitro assembly of type I collagen from rat tail tendon is a multistep process (1-3). Step 1 (initiation) is temperature-dependent but complete in 6 min at 26°

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Author

R.A. Gelman; K.A. Piez

Publisher

Elsevier BV

Published

1980

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)