Electrophoretic profile, mobility and relative proportions of major anterior pituitary tissue extractable and secretory proteins of domestic water buffalo were compared with these of cattle, sheep, goat, pig, rabbit and rat using polyacrylamide. In 7.5% gels, 2 major bands corresponding to growth hormone (GH) and prolactin (PRL) were obtained in all the cases. The relative electrophoretic mobility of GH from buffalo, ox, sheep and goat was similar. Rabbit and rat GH had highest mobility. In 10% gels, 3 distinct major protein bands were obtained in all the species. The additional band having intermediate mobility between GH and PRL was named as albumin like protein (ALP). The relative proportions of the tissue extractable and secretory GH, PRL, ALP and others showed no uniform pattern but ALP and PRL were in general higher than GH except in sheep and goat. The rate of secretion of GH in vitro was also lower as compared to ALP and PRL. The major adenohypophyseal proteins although similar in cattle and buffalo, were considerably different from those of nonruminants.