Transferrin description

The most detailed description of a complete transferrin molecule is that of human lactoferrin, at 2.8-A resolution (78), and most of the data in the following sections come from this work and from refinement of the same structure at 2.1-A resolution (79). As would be expected from the high level of sequence similarity, the three-dimensional structure of rabbit serum transferrin (68), although at lower resolution (3.3 A), is completely consistent with that of lactoferrin the differences are at the level of individual amino acid changes, together with some differences in lobe and domain orientations. These are discussed below (Section III.B.l). 

Consequently, the present chapter does not deliver any information about the structure function relationships of transferrin s glycans. However, it is devoted to an interesting study of horizontal evolution through the superfamily of transferrins. In this respect, the present chapter is a useful addition to chapters 6-12 of volume 29A [15] and to chapters 1-8 of the present volume [16]. In fact, these chapters are devoted to the description of the primary structure of glycoprotein glycans from bacteria to man and are thus relevant to vertical evolution . 

Since the original description of Detrisac et al. [46] a 1 1 mixture of DMEM and HAMF12, supplemented with hydrocortisone, triiodothyronine, insulin, transferrin and selenate (currently known as K1 medium) [51], has been the most widely used medium in human (proximal) tubular epithelial cell culture. Several authors add serum because of its growth promoting effect. 

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