The present investigation has dealt with biochemical studies of an important medicinal plant, Mucuna pruriens L. of Fabaceae. This plant synthesizes L-dopa, a neurotransmitter precursor, which is used in Parkinson’s disease and other mental disorders. The biochemical study involves total protein analysis and activities of two isozymes in both in vitro regenerates and field grown plants of two varieties of M. pruriens, M. pruriens var pruriens and M. pruriens var. utilis. A remarkable increase in total protein content with increased number of polypeptide bands, as observed in qualitative protein profile study has been observed in the regenerates as compared to field grown plants which may be attributed to the high level of different enzyme activities. Also, differences exist in protein profile among strains of these two varieties revealing genomic diversity. The activities of both esterase and peroxidase isozymes have also been augmented in the regenerates showing more number of isoforms in comparison to field grown plants. The differential level of gene expression might have been responsible for such elevated levels of proteins and isozymes activities.