Normal human hyaline cartilages contain five distinguishable coltagenous proteins in addition to, and different from the αl(II) chain of Type II collagen. This report describes the characterization of three of these additional proteins. By the criteria of solubility, electrophoretic mobilities, ion-exchange and sieve chromatographic properties, amino acid compositions, and cyanogen bromide peptide profiles, at least two of these proteins, and possibly the third, are structurally distinct collagen α chains different from previously reported collagen chains. These findings imply further molecular heterogeneity of vertebrate collagens, and the existence of at least 9 different structural genes for collagen chains. © 1979 Academic Press, Inc. All rights of reproduction in any form reserved.