The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains.

@article{Muragaki1990TheCP,
  title={The complete primary structure of two distinct forms of human alpha 1 (IX) collagen chains.},
  author={Yasuteru Muragaki and Tomoatsu Kimura and Yoshifumi Ninomiya and Bjorn Reino Olsen},
  journal={European journal of biochemistry},
  year={1990},
  volume={192 3},
  pages={703-8}
}
Type IX collagen molecules contain three genetically distinct subunits. One of the subunits, alpha 2(IX), contains a covalently attached glycosaminoglycan side chain. A second subunit, alpha 1 (IX), has been found to be synthesized in two forms. The two forms are generated by the alternative use of two transcription start sites and splice patterns. The two forms have been found in chicken, mouse and human but cDNAs encoding both forms have only been reported for chicken. In the present report… CONTINUE READING