The problem of age gelation in ultra-high temperature (U1IT) sterilized milk retentate (ultrafiltered 3x concentrated) is investigated in this work. Transmission electron microscopy (1EM), utilizing the microcube encapsulation technique and protocols for immunolocalization of milk proteins, provides insight into the phenomenon of age gelation ofUHT-sterilized, ultrafiltered (UF) milk retentate. Primary antibodies (specific for the native as well as the complexed forms of milk proteins) and secondary antibodies (conjugated to gold probes) are used to elucidate the positions of the milk proteins in various samples of milk from the stage of milking through UHT sterilization and storage for 12 months, by which time gelation had occurred. The movement of the milk proteins is charted and these data are used to determine the role of the proteins in age gelation of UHT-sterilized UF milk retentate. Heat-denatured β-lactoglobulin and α-lactalbumin form complexes within the serum as well as with the casein components of the micelles. UHT sterilization not only denatures β-lactoglobulin and α-lactalbumin, but catalyzes the reaction of these whey proteins and K-casein, leading to the successful formation of the complex. Complexing of β-lactoglobulin and K-casein competitively weakens the complex of K-casein to other casein fractions of the micelle. This leads to migration of K-casein from the micelle to the serum, compromising the role of K-casein in stabilizing the casein proteins within the micellar moiety. The time-dependent loss of K-casein from the micelle would expose the calcium-insoluble micellar αs1-casein and β-casein to the serum calcium. Subsequent to this, some αs1-casein and β-casein are also released from the micelles, and gelation of the milk occurs. No information was obtained on location of αs2-casein. The release of K-casein from the micelles thus apparently represents the critical factor in the phenomenon of age gelation in UHT-sterilized milk concentrates.