The polypeptide chain of human lactotransferrin possesses two glycosylation sites to which glycans are linked through an N-(P-asparty1)-N-acetylglucosaminylamine bond and which are structurally heterogenous. After chymotryptic or pronase digestions, glycopeptides with five different glycan structures could be isolated. For three of them, the structure has been determined by the application of methanolysis, methylation analysis, hydrazinolysis/nitrous deamination, enzymatic cleavage and 'H-NMR spectroscopy at 360 MHz: Glycopeptides A and B : NeuAc(cr2-6)Gal(~1-4)GlcNAc(~l-2)Man(crl-3) shows that important differences exist between the number and the structure of the glycans present in these four kinds of transferrins.In the case of human lactotransferrin, in 1966, the presence of two glycans linked by a 4-N-(2-acetamido-2-deoxy-B-~-glucopyranosy1)-L-asparagine linkage was described as well as one 0-glycosidically-linked glycan [17]. The presence of two N-glycosidically-linked glycans was confirmed in 1973 and for one of them the structure was proposed [18].Microheterogeneity of the carbohydrate moieties was later demonstrated and partial results concerning different glycan structures were given in general reviews [19-211. In the present paper we describe the complete primary structure of three types of glycans as determined by methanolysis, methylation analysis, hydrazinolysis/nitrous deamination, mass spectrometry, enzymatic cleavage and 'H-NMR spectroscopy at [111._.___