Abstract
Vitrosin, a fibrous protein obtained from the vitreous humor of the eye in the form of an indefinitely long fibril about 100 to 150 A in diameter, has been identified as a member of the collagen class of proteins. It is characterized by the collagen wide-angle x-ray diffraction pattern, and axial periodicity of about 640 A determined by electron microscopy and small-angle x-ray diffraction, an amino acid pattern characteristic of collagen as determined by paper chromatography, and a hydroxyproline and glycine content also typical of collagen. The glycine-hydroxyproline ratio is somewhat lower than that for most vertebrate collagens.
Full Text
The Full Text of this article is available as a PDF (617.8 KB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- BEAR R. S. The structure of collagen fibrils. Adv Protein Chem. 1952;7:69–160. doi: 10.1016/s0065-3233(08)60018-2. [DOI] [PubMed] [Google Scholar]
- GROSS J., HIGHBERGER J. H., SCHMITT F. O. Some factors involved in the fibrogenesis of collagen in vitro. Proc Soc Exp Biol Med. 1952 Jul;80(3):462–465. doi: 10.3181/00379727-80-19657. [DOI] [PubMed] [Google Scholar]
- MARKS M. H., BEAR R. S., BLAKE C. H. X-ray diffraction evidence of collagen-type protein fibers in the Echinodermata, Coelenterata and Porifera. J Exp Zool. 1949 Jun;111(1):55–78. doi: 10.1002/jez.1401110104. [DOI] [PubMed] [Google Scholar]
- MARTIN C. J., AXELROD A. E. A modified method for determination of hydroxyproline. Proc Soc Exp Biol Med. 1953 Jul;83(3):461–462. doi: 10.3181/00379727-83-20386. [DOI] [PubMed] [Google Scholar]
- MATOLTSY A. G. Analysis of the ultrastructure of vitrosin fibers on the basis of the polarization optical method. Biochim Biophys Acta. 1953 Jul;11(3):326–328. [PubMed] [Google Scholar]
- MATOLTSY A. G., GROSS J., GRIGNOLO A. A study of the fibrous components of the vitreous body of the electron microscope. Proc Soc Exp Biol Med. 1951 Apr;76(4):857–860. doi: 10.3181/00379727-76-18655. [DOI] [PubMed] [Google Scholar]
- NEUMAN R. E., LOGAN M. A. The determination of hydroxyproline. J Biol Chem. 1950 May;184(1):299–306. [PubMed] [Google Scholar]
- NEUMAN R. E. The amino acid composition of gelatins, collagens and elastins from different sources. Arch Biochem. 1949 Dec;24(2):289–298. [PubMed] [Google Scholar]
- REDFIELD R. R. Two-dimensional paper chromatographic systems with high resolving power for amino acids. Biochim Biophys Acta. 1953 Feb;10(2):344–345. doi: 10.1016/0006-3002(53)90260-1. [DOI] [PubMed] [Google Scholar]
- SCHWARZ W. Die Gelkörperfibrillen des menschlichen Glaskörpers. Z Zellforsch Mikrosk Anat. 1951;36(3):284–292. [PubMed] [Google Scholar]
- SCHWARZ W., SCHUCHARDT E. Die Struktur des frischen Glaskörpers; Untersuchungen im Phasenkontrast-, Dunkelfeld- und Immersions- Ultramikroskop. Z Zellforsch Mikrosk Anat. 1950;35(3-4):293–310. [PubMed] [Google Scholar]
- YOUNG R. G., WILLIAMS H. H. Biochemistry of the eye. II. Gelatinous protein of vitreous body. AMA Arch Ophthalmol. 1954 May;51(5):593–595. doi: 10.1001/archopht.1954.00920040603003. [DOI] [PubMed] [Google Scholar]
- Young R. A. The Ground Substance of Connective Tissue. J Physiol. 1894 May 29;16(5-6):325–350. doi: 10.1113/jphysiol.1894.sp000505. [DOI] [PMC free article] [PubMed] [Google Scholar]
