Comparison of axial banding patterns in fibrils of type V collagen and type I collagen.

Type V collagen and type I collagen were obtained from human placenta, essentially by salt fractionation. Precipitates were formed from mixed solutions of type V collagen and type I collagen in various ratios. They were incubated at 37 degrees C for 1 hour and negatively stained with 0.5% uranyl acetate (pH 4.4) at 37 degrees C. The specimens, seen by electron microscopy, were fibrils with a D-periodic banding pattern. Axial electron density profiles of collagen fibrils were obtained from selected electron micrographs by densitometric tracing. The slit width corresponded to 1.5 nm. The relative electron densities of overlap region vs. hole region were lower than 20% in fine fibrils containing a significant amount of type V collagen. It is suggested that the overlap region of such collagen fibrils may be loosely packed, being accessible to uranyl acetate, or the hole region may be filled by larger non-collagenous portions of type V collagen, resulting in loss of the light and dark alternation. Six to 8 white transverse lines were discerned per period and labeled consecutively with Arabic numerals. White lines 2 and 5 tended to merge with lines 1 and 4, respectively, in collagen fibrils formed from a solution containing a significant amount of type I collagen or pure type I collagen. The eight white lines corresponded to c2, c1, b2, b1, a4, a1, e1 and d with reference to their locations in the D-period. The locations of white lines in collagen fibrils which contain significant amount of type V collagen were identical with those in type I collagen fibrils. This is consistent with the primary structure that the axial distribution of charged amino acids in type V collagen is quite similar to that in type I collagen.