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兔网织红细胞无法摄取伴清蛋白或乳铁传递蛋白中的铁。

Failure of rabbit reticulocytes to incorporate conalbumin or lactoferrin iron.

作者信息

Zapolski E J, Princiotto J V

出版信息

Biochim Biophys Acta. 1976 Jan 14;421(1):80-6. doi: 10.1016/0304-4165(76)90171-9.

Abstract

Despite the remarkable molecular similarity of human lactoferrin and human transferrin, the results of this investigation indicate that human lactoferrin was unable to furnish rabbit reticulocytes with iron for heme synthesis. Although conalbumin closely resembles transferrin in many of its properties, conalbumin iron-binding differs from human transferrin iron-binding. There are conflicting reports in the literature regarding conalbumin's ability to furnish iron to reticulocytes. In this study, small amounts of lactoferrin or conalbumin were adsorbed to mature and immature cell surfaces but neither of these iron-binding proteins surrendered iron intracellularly to reticulocytes for heme synthesis.

摘要

尽管人乳铁蛋白与人转铁蛋白在分子结构上极为相似,但本次研究结果表明,人乳铁蛋白无法为兔网织红细胞提供用于血红素合成的铁。虽然伴清蛋白在许多特性上与转铁蛋白极为相似,但其铁结合方式与人转铁蛋白的铁结合方式不同。关于伴清蛋白向网织红细胞提供铁的能力,文献中有相互矛盾的报道。在本研究中,少量乳铁蛋白或伴清蛋白吸附于成熟和未成熟细胞表面,但这两种铁结合蛋白均未在细胞内将铁传递给网织红细胞用于血红素合成。

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