Abstract
1. 1. Pepsin insensitive fragments of collalgen extracted from tube feet and peristome have α 1 and α 2 bands that differ in apparent molecular weights from each other and from human type 1 collagen. 2. 2. A monoclonal antibody that reacts with the ξ I band and a low molecular weight fragment of tube foot collagen does not react with either peristome collagen or human type I collagen. 3. 3. Measurements of the axial periodicity of native fibers of tube foot and peristone collagens indicate they have D values that differ significantly from each other and from reported values of vertebrate type I collagen. 4. 4. We propose that there are diverse and specialized types of collagen in sea urchins that are heterogeneously distributed in the extracellular matrix of different tissue.
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