Abstract
ABSTRACTMajor hemolymph protein (MHP) was purified from larval hemolymph of Galleria mellonella by KBr density gradient ultracentrifugation, ion exchange chromatography (DEAE‐Trisacryl M), YM‐50 ultrafiltration and gel permeation chromatography (Sephadex G‐100). MHP is composed of two subunit (MHP‐1 and MHP‐2). The molecular weights of each subunit were determined (MHP‐1 = 86 kDa and MHP‐2 = 84 kDa). MHP is present in both hemolymph and fat body during developmental stages, indicating this protein is carrying out some functions different from other major protein such as storage protein and lipophorin.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
