A process for virus isolation and purification via immunoaffinity chromatography wherein the said process is consisting of the following steps (i)-(iv): (i) binding the antibody to the chromatographic stationary phase; the antibody is specific for a surface protein of the virus which is subjected to the said purifying process; the binding is achieved by conventional techniques of covalent binding which results in formation of the column for immunoaffinity chromatography; (ii) then the said chromatographic column from the step (i) is: (a) equilibrated by flushing it with the solution of binding buffer consisting of: 20 mM of 3- (N-morpholino) propanesulfonic acid, 0.15 M sodium chloride at pH= 7.2-7.4; followed by (b) loading of the starting suspension of contaminated viruses which is intended to be purified onto such equilibrated chromatographic column; (iii) washing of contaminants and non-bonded viruses out of the column by flushing it with the same binding buffer from the step (ii); and (iv) elution of the purified virus bounded on the stationary phase of the column; characterized by that, the said elution is performed by using the mobile phase which is a solution consisting of ingredients A.-D. as indicated below: A. one or more amino acids selected from: L-serine <1>, L-asparagine <2>, L-glutamine <3>, or their salts with pharmaceutically acceptable acids; B. one or more ingredients selected from: L-arginine, glycine, imidazole, or their salts with pharmaceutically acceptable acids; C. one or more pharmaceutically acceptable pH adjusting agents, acid or base, suitable for adjusting the pH value of the said mobile phase to pH= 6.0-8.0; and D. purified water; up to 100% w/w of the said mobile phase composition; and where said elution gives an eluate in the form of a suspension of purified virus in the said mobile phase. (i) binding the antibody to the chromatographic stationary phase; the antibody is specific for a surface protein of the virus which is subjected to the said purifying process; the binding is achieved by conventional techniques of covalent binding which results in formation of the column for immunoaffinity chromatography; (ii) then the said chromatographic column from the step (i) is: (a) equilibrated by flushing it with the solution of binding buffer consisting of: 20 mM of 3- (N-morpholino) propanesulfonic acid, 0.15 M sodium chloride at pH= 7.2-7.4; followed by (b) loading of the starting suspension of contaminated viruses which is intended to be purified onto such equilibrated chromatographic column; (a) equilibrated by flushing it with the solution of binding buffer consisting of: 20 mM of 3- (N-morpholino) propanesulfonic acid, 0.15 M sodium chloride at pH= 7.2-7.4; followed by (b) loading of the starting suspension of contaminated viruses which is intended to be purified onto such equilibrated chromatographic column; (iii) washing of contaminants and non-bonded viruses out of the column by flushing it with the same binding buffer from the step (ii); and (iv) elution of the purified virus bounded on the stationary phase of the column; A. one or more amino acids selected from: L-serine <1>, L-asparagine <2>, L-glutamine <3>, or their salts with pharmaceutically acceptable acids; B. one or more ingredients selected from: L-arginine, glycine, imidazole, or their salts with pharmaceutically acceptable acids; C. one or more pharmaceutically acceptable pH adjusting agents, acid or base, suitable for adjusting the pH value of the said mobile phase to pH= 6.0-8.0; and D. purified water; up to 100% w/w of the said mobile phase composition; and