In order to identify the mucins synthesized and secreted in the rat co
lon, we studied their biochemical characteristics and biosynthesis and
evaluated their analogy to human colonic mucins. Purified mucin from
both species appeared similar with respect to composition, buoyant den
sity and mobility on SDS/PAGE. Isolated rat colonic mucin (RCM) was us
ed to elicit a polyclonal antiserum, which was used in metabolic label
ling studies to identify mucins and mucin precursors. RCM is synthesiz
ed as a 600 kDa precursor protein, which oligomerizes before O-glycosy
lation. The mature, high-molecular mass mucin is secreted and displays
an anomalous molecular mass on SDS/PAGE of approximately 650 kDa. Pol
ymorphism in precursor size was found among different rats, suggesting
genetic heterogeneity. Molecular mass, biosynthesis and secretion of
RCM appeared similar to human MUC2. Moreover, RCM precursor could be i
mmunoprecipitated using specific anti-(human MUC2) antisera, indicatin
g that the RCM can be designated rat MUC2. This study describes the bi
osynthesis of two homologous mucins in two different species. The high
degree of similarity suggests functional analogy.