락토페린 구조 기능 및 생산에 관한 연구 = Studies on the Structure , Function and Production of Lactoferrin

다국어 초록 (Multilingual Abstract)

Lactoferrin is an 80 kDa, iron-binding glycoprotein present in milk and, to a lesser extent, in exocrine fluids such as bile and tears. It consists of a single-chain polypeptide with two globular lobes and is relatively resistant to proteolysis. Owing to its iron-binding properties, lactoferrin has been proposed to play a role in iron uptake by the intestinal mucosa and to act as a bacteriostatic agent by withholding iron from iron-requiring bacteria. Beside this, the functions proposed for lactoferrin are diverse and include immunomodulatory activity, regulation of myelopoiesis, cell growth promotion and differentiation, and antioxidant effects. Therefore lactoferrin has been a good target for commercial production. Until now lactoferrin has been purified from human, bovine, sheep, goat and horse milk. Complete amino acid sequences of the lactoferrin from human, murine, bovine, porcine, and caprine have been determined, either directly at the protein level or deduced from the nucleotide sequence and shown to display a high level of similarity. We, researchers in my laboratory, have been studied lactoferrin for mass production by using the techniques of transgenic animal, transgenic plant and microorganism. Here we present the data on structure, function and production of lactoferrin.