Isolation of immunoreactive proteins from the larval extracts of Boophilus microplus and Hyalomma anatolicum anatolicum

Abstract

Crude larval antigens of Boophilus microplus (LEB) and Hyalomma a. anatolicum (LMS) were purified by gel filtration and anion-exchange chromatography to isolate the immunoreactive antigens responsible for induction of resistance. Gel filtration and DEAE-sepharose chromatography of LEB yielded 120 and 76 fractions, respectively, but only one collected by 0.2 M NaCl showed significant precipitation reactions. Similarly, by sephadex G-200 filtration followed by anionexchange chromatography of LMS, an immunoreactive fraction was isolated. Sodium dodecyl sulphate polyacrylamide gel electrophoresis of reactive fractions showed a 68 kDa protein in LEB and 62 and 29 kDa proteins in LMS. The study presents physicochemical procedures for the purification of tick proteins.