The activity or correct antigenic conformation of complex glycoprotein, most of the times require of the biosynthetic machinery of higher cells.  Thus the recombinant production of these proteins most be performed in stably transformed insect, plant or mammalian cells. However, as a general rule, all these expression system require of a relatively long time between the addition of the desire DNA sequence and the obtaining of a high producing clone. Here we assess the use of adenoviral vectors as way to produce large quantities of recombinant proteins. By the use of adenoviral vectors, we have been able to express several recombinant proteins both in transduced mammalian cell cultures and in the milk of non transgenic goat.  Direct transduction of mammalian cell cultures have allowed us to obtain human grown hormone in the culture medium at a concentration of up to 0.7 mg/ml, human EPO at level of up to 0.25 mg/ml, E2 gycoprotein (from classical swine fever virus) at levels of up to 0.45 mg/ml. All these protein were also expressed in the mammary gland of non-transgenic goat at level of 0.8 g/L, 2.5 g/L and up to 1 g/L of hGH, hEPO and E2 respectively. The procedure here described is a very fast and easy way to produce complex recombinant protein in quantities high enough to perform most of the laboratory or preclinical assay required before undertake the stable modification of an animal or cell line.