ABSTRACT
The accuracy of a maternity assessment based on visual observation was tested during the post parturient phase in farmed red deer. The mother of the calf was determined using visual observation of the hind's peri-parturient and early maternal behaviour during the first week of the calf's life. This assessment was compared with genetic analysis based on DNA microsatellite polymorphism. Data for 48 new-born calves and 50 hinds were compared. The visual assessment of maternity was correct in 43 of the 48 cases (89.58%). In the five remaining cases the mother was identified by DNA testing whereas adoptive mother was determined by visual observation. Altogether 14 cases of adoption were seen in this study and in 9 cases the biological mother was correctly determined by visual observation. Detailed observation of the hind-calf interactions during calving and the first week after the parturition allowed an accurate prediction of maternity. However, such observation is technically demanding.
ABSTRACT
Serum samples of Meishan (13 animals) and Meishan x Wild Boar crosses (361 animals) were analysed by means of two-dimensional electrophoresis. Some new variants in protease inhibitor systems PO1A, PO1B and PI2 are reported.
Subject(s)
Genetic Variation , Protease Inhibitors/blood , Swine/genetics , Animals , Crosses, Genetic , Female , Male , Swine/bloodABSTRACT
Three related alpha-protease inhibitors, PI2 I, PI3 C and PI4 C2, of blood serum of the pig (Sus scrofa) were isolated. PI2 I inhibited both trypsin and chymotrypsin; PI3 C and PI4 C2 strongly inhibited chymotrypsin, but did not significantly inhibit trypsin. By using SDS-PAGE, the three proteins were found to be composed of single polypeptide chains, and molecular weights were 63,000 for PI2 I, 58,000 for PI3 C and 64,000 for PI4 C2. All three proteins were shown to be glycoproteins. In PI3 C, eight sialic acid residues were found, and in PI4 C2 (similarly as in PI2 F) 10-11 residues were found. Amino acid composition as well as N-terminal sequences of the three proteins were very similar, indicating close homology. Comparison of these partial amino acid sequences with the cDNA-deduced amino acid sequence of pig alpha-antichymotrypsin (AACT; Buchman, 1989, GenBank, Accession No. M29508) revealed great similarities, the sequence of PI2 I being virtually identical with the pig AACT. On the basis of all available results, PI2 is proposed to be pig AACT, an orthologue of human AACT.
