Origin of late lactation protein from beta-lactoglobulin in the tammar wallaby.

Abstract

Two of the dominant whey proteins of the tammar wallaby, beta-lactoglobulin (BLG) and late lactation protein (LLP), have been positively identified on gradient polyacrylamide gradient gels by N-terminal protein sequencing. The origin of the electrophoretic variation present in these proteins has been found to be principally genetic. The variation was examined in 97 lactating female tammar wallabies, of which 10 were followed throughout lactation to determine if any developmental variation existed. The only distinguishable developmental difference results from the previously described appearance of LLP at the beginning of phase III of lactation (approximately 180 days after birth of the young). Electrophoretic analysis of BLG implies that it exists in monomeric, dimeric, and tetrameric forms. Very strong linkage disequilibrium, indicative of close linkage, was found between alleles at the Blg and Llp loci. Examination of their cDNA sequences suggests that LLP and BLG represent an ancient gene duplication. Both have conserved amino acid residues characteristic of the lipocalins. The results imply that the marsupial mode of lactation, and hence of reproduction, is also very ancient.