Van Bockxmeer F M, Martin C E, Constable I J
Biochim Biophys Acta. 1983 Jul 5;758(1):17-23. doi: 10.1016/0304-4165(83)90004-1.
The soluble protein composition of Macaque monkey vitreous humour was studied in order to understand its iron-binding properties. The protein content of vitreous humour was 217 micrograms/ml +/- 4.6%, 40% of which was serum albumin and 30% an iron-binding protein of hydrodynamic properties identical to that of transferrin or lactoferrin. Relative to serum, the vitreous humour contained a 13-fold excess of this protein(s). Isoelectric focusing, iron-binding and immunoelectrophoretic studies indicated that both vitreous humour and aqueous humour contained lactoferrin as well as serum transferrin. The iron-binding capacity of these proteins in vitreous humour was equivalent to the mass of haemoglobin iron contained in at least 570000 monkey erythrocytes. It was concluded that the intraocular lactoferrin originated from within the eye. These iron-binding proteins may play a protective role in ocular disturbances such as vitreous haemorrhage, iron foreign body toxicity and infection.
为了解猕猴玻璃体液的铁结合特性，对其可溶性蛋白质组成进行了研究。玻璃体液的蛋白质含量为217微克/毫升±4.6%，其中40%为血清白蛋白，30%为一种铁结合蛋白，其流体动力学性质与转铁蛋白或乳铁蛋白相同。相对于血清，玻璃体液中这种蛋白质的含量高出13倍。等电聚焦、铁结合和免疫电泳研究表明，玻璃体液和房水都含有乳铁蛋白以及血清转铁蛋白。这些蛋白质在玻璃体液中的铁结合能力相当于至少570000个猴红细胞中所含血红蛋白铁的质量。得出的结论是，眼内乳铁蛋白源自眼内。这些铁结合蛋白可能在玻璃体出血、铁异物毒性和感染等眼部疾病中发挥保护作用。
