K. Simpson et al., DEVELOPMENTALLY-REGULATED EXPRESSION OF A PUTATIVE PROTEASE INHIBITORGENE IN THE LACTATING MAMMARY-GLAND OF THE TAMMAR WALLABY, MACROPUS-EUGENII, Comparative biochemistry and physiology. B. Comparative biochemistry, 120(3), 1998, pp. 535-541
A novel milk protein, which is secreted only in the early stage of lac
tation, has been identified in the whey fraction of milk from the tamm
ar wallaby (Macropus eugenii). The amino acid sequence currently avail
able suggests the protein comprises 71 amino acids. The protein migrat
es at 18 kDa when analysed by SDS polyacrylamide gel electrophoresis b
ut has a calculated molecular weight of 8 kDa. A partial cDNA clone of
153 bp has been isolated by reverse transcriptase PCR. Northern analy
sis of mammary gland RNA extracted from various stages throughout the
entire lactation period showed a messenger RNA transcript of approxima
tely 500 bp present only in the first third of lactation. The protein
shares 74.5% similarity at the amino acid level with early lactation p
rotein (ELP) from the brush-tailed possum (Trichosurus vulpecula) and
37% with bovine colostrum trypsin inhibitor, a member of the Kunitz fa
mily of protease inhibitors. We hypothesise that the expression of thi
s gene may be controlled by changes in the sucking patterns of the dep
endent pouch young. (C) 1998 Elsevier Science Inc. All rights reserved
.