Chinese hamster lung cells synthesize and confine to the cellular domain a collagen composed solely of B chains.

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Abstract
The acid-soluble collagen extracted from cultured Chinese hamster lung (CHL) cell layers was isolated after limited pepsin digestion and differential salt fractionation. Polyacrylamide gel electrophoresis of this material under denaturing conditions showed the presence of collagen chains with an apparent molecular mass of 120,000 daltons both before and after reduction, indicating the absence of interchain disulfide bonds in the native molecule. When chromatographed on CM-cellulose under denaturing conditions, the majority (> 90%) of the CHL cell layer collagen eluted as relatively basic components slightly before the human .alpha.2(I) chain and coincident with the human B chain. CM-cellulose elution profiles of the CNBr peptides derived from the human B chain and from the CHL cell layer chain were essentially identical. Examination of CHL cells in culture by using affinity-purified antibody to human B chain revealed this collagen to be localized in an extracellular matrix surrounding the cells. Analysis of the culture medium indicated the absence of any comparable collagen chain. Apparently, there is a molecular form of collagen composed solely of B chains. Apparently this molecular form of collagen has an unusual affinity for the cell layer in this system.