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B W Streeten, D A Swann, P A Licari, M R Robinson, S A Gibson, N J Marsh, J P Vergnes, I L Freeman; The protein composition of the ocular zonules.. Invest. Ophthalmol. Vis. Sci. 1983;24(1):119-123.
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Bovine and human zonules were found to be composed of noncollagenous acidic glycoprotein with a high cysteine content, double that previously reported. In reduced zonular fractions the most prominent peptide had a molecular weight (MW) of approximately 70,000. Lesser quantities of 170,000, 50,000, and 35,000 dalton peptides were also present and a variable number of lower MW bands, depending upon the degree of reduction and denaturation. A fraction of bovine zonules soluble in low ionic strength buffers contained primarily a peptide of approximately 50,000 daltons, often present as a doublet. Amino acid and hexosamine content of these two fractions was consistent with the presence of at least two different glycoconjugates, one a proteoglycan. Carbohydrate analysis of whole zonules suggested that these glycoconjugates include a sialofucose-containing glycoprotein and a lesser quantity of xylose-containing proteoglycan. The amino acid profile and peptide content of the zonules resembled that of elastic tissue microfibrils, increasing further the possibility of a close relationship between these two fibrils.
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