Pierre Jolles

The present state of the human lactotransferrin sequence: Study and alignment of the cyanogen bromide fragments and characterization of N- and C-terminal domains

Human lactotransferrin contains six residues of methionine per mol. Seven different fragments were characterized after treatment with cyanogen bromide (CNBr) and large parts of their sequences were determined. The alignment of the CNBr fragments was established by the determination of N- and C-terminal sequences, by the study of the C-terminal domain obtained by peptic digestion of the protein and by taking into account the internal homology as well as homology with human serum transferrin. The two glycopeptides were situated in the N- and C-terminal parts of the protein, respectively, a situation quite different from that encountered in serum transferrin. The sequence studies allowed us to suggest a 4- and perhaps 6-fold internal homology.

Cyclic phosphorylation/dephosphorylation cascade in bovine brain coated vesicles

Coated vesicles are involved in transport of membrane proteins between several intracellular membrane-bound compartments. These vesicles possess a specific 50-kDa protein which is phosphorylated and dephosphorylated by a coated-vesicle-specific kinase and phosphatase. We studied this phosphorylation/dephosphorylation cascade system and show that the phosphorylation level of the 50-kDa protein is governed by the ATP/ADP ratio.