This study was conducted to establish the normal dimensions of the different segments of the female r eproductive tract of the Black Bengal goats. The reproductive tracts of 56 adult non-gravid, female Black Bengal goat were collected and biometric parameters of different segments of the female reproductive tracts i.e. vulva, vagina, cervix, uterine body, uterine horns, oviducts and ovaries were measured .The lengths of the right and left ovaries were 1.453±0.034 and 1.410±0.026 cm, respectively. Mean weight of left ovary was 0.5944±0.06 gm and that of right ovary was 0.614±0.07 gm in Black Bengal goat. The average numbers of follicle in right and left ovaries were 4.123±0.230 and 3.893±0.229, respectively. The mean lengths of the vulva, vagina, cervix, uterine body, uterine horns and oviduct were 2.671±0.063, 7.132±0.165, 3.348±0.113, 2.50±0.112 and 12.287±0.270 and 10.150±0.228 cm, respectively. The width of the vagina, cervix, uterine body and uterine horn were 3.972±0.098, 1.7551±0.042, 2.739±0.079 and 2.805±0.069 cm, respectively. The average number of curuncle in uterus was 54.714±1.70. A significant difference (p<0.05) between right and left ovaries was found for ovario-bursal adhesion. The mean weight, length and width in the present study were found higher in right ovaries than those of left ovaries.

A panel of monoclonal antibodies (MoAbs) against cell surface proteins of early BFUe progeny was characterized. Five of these antibodies (Abs) reacted with normal erythroid, but not myeloid, bone marrow cells. Each of the five antibodies, typified by Ab 69.20, immunoprecipitated a dimeric complex of 185,000, which is composed of two identical disulfide-bonded subunits. This antigen had affinity for transferrin, and was essentially identical in biochemical characteristics to transferrin receptors precipitated with the well-characterized MoAbs OKT9 and 5E9. However, this form of transferrin receptor lacked both the OKT9 and 5E9 antigenic determinants and, moreover, the 69.20 epitope was absent from the conventional transferrin receptor, as defined by Abs OKT9 and 5E9. Modulation experiments demonstrated that both 69.20 and OKT9 modulated large, virtually independent populations of transferrin receptors. Both forms of transferrin receptor appeared to be derived from the product of a single gene, but the form defined by MoAb 69.20 apparently predominates in cells of the erythroid lineage and some transformed cell types that manifest a special requirement for iron. These data suggest that cells with a high iron requirement synthesize two forms of transferrin receptor, possibly by means of differential mRNA splicing or by posttranslational modification of the transferrin receptor.

A panel of monoclonal antibodies (MoAbs) against cell surface proteins of early BFUe progeny was characterized. Five of these antibodies (Abs) reacted with normal erythroid, but not myeloid, bone marrow cells. Each of the five antibodies, typified by Ab 69.20, immunoprecipitated a dimeric complex of 185,000, which is composed of two identical disulfide-bonded subunits. This antigen had affinity for transferrin, and was essentially identical in biochemical characteristics to transferrin receptors precipitated with the well-characterized MoAbs OKT9 and 5E9. However, this form of transferrin receptor lacked both the OKT9 and 5E9 antigenic determinants and, moreover, the 69.20 epitope was absent from the conventional transferrin receptor, as defined by Abs OKT9 and 5E9. Modulation experiments demonstrated that both 69.20 and OKT9 modulated large, virtually independent populations of transferrin receptors. Both forms of transferrin receptor appeared to be derived from the product of a single gene, but the form defined by MoAb 69.20 apparently predominates in cells of the erythroid lineage and some transformed cell types that manifest a special requirement for iron. These data suggest that cells with a high iron requirement synthesize two forms of transferrin receptor, possibly by means of differential mRNA splicing or by posttranslational modification of the transferrin receptor.

A cytotoxic (IgG2b) monoclonal antibody (McAb) for a novel erythroid differentiation antigen was generated by hyperimmunizing young mice with mononuclear cells obtained from livers of 20- to 22-week-old fetuses. This McAb, designated SFL 23.6, shows an extremely well- defined reactivity with the cells of the erythroid lineage at all stages of maturation as evident from the labeling of morphologically identifiable erythroid precursors and of erythrocytes present in peripheral blood, bone marrow, and fetal liver, and from its reactivity with culture-derived erythroblasts. The nonerythroid cells present in these and other tissue preparations were not labeled by SFL 23.6. The erythroid lineage specificity of McAb SFL 23.6 was confirmed by a cell- sorting experiment in which 97% of the cells in the fluorescent fraction sorted from SFL 23.6-treated bone marrow cells were erythroid precursors at various stages of maturation. Complement-mediated cytotoxicity and progenitor cell-sorting experiments showed that most (greater than 90%) of the late erythroid progenitors (CFU-E) and only a small proportion of the early erythroid progenitors (BFU-E) express the antigenic determinant identified by SFL 23.6. The myeloid progenitors (CFU-GM) and multilineage progenitors (CFU-GEMM) were negative for the SFL 23.6 antigenic determinant. The antigen recognized by SFL 23.6 has not been determined as yet. Because of the pattern of its reactivity and its dependence on sialic acid residues, the possibility of its relationship to glycophoria A was entertained. However, previous work using antiglycophorin McAbs (R-10) has shown that this determinant is not expressed in CFU-E. Therefore, among the erythroid lineage-specific McAbs described thus far, SFL 23.6 is unique in its reactivity with CFU- E and the mature erythron. Reagents with such specificity may be useful in studies of erythroid differentiation and commitment.