Acid alpha-D-mannosidase from turkey seminal plasma

Five multiple forms of alpha-D-mannosidase from turkey seminal plasma were separated by chromatofocusing. The enzyme forms yielded different native M(r) and pI values. Other biochemical properties such as optimum pH, the Km values, thermal stability at 65 degrees C, and the effect of some ionic compounds and carbohydrates on the enzyme activity were similar for all forms.