Tissue site and modification of a bacteria-induced coagulation protein from Manduca sexta

Michael F. Minnick, Kemet D. Spence

Research output: Contribution to journalArticlepeer-review

13 Scopus citations


Isolated naive and immune tissues of M. sexta larvae were extracted, electrophoresed and immunoblotted to screen for the presence of a bacteria-induced coagulation-initiating protein termed M13. Immunoblots developed with anti-M13 antiserum show that M13 (36K) can be detected in naive hemolymph, and in hemolymph, epidermis and midgut tissues isolated from immune insects. M13 was not detected in the hemocytes or fat bodies from either naive or immune insects. A lower molecular weight (33K) cross-reactive protein termed 33K-CRP was also detected in hemolymph and epidermis samples, and data suggest that it may represent a partial proteolysis product of M13. The apparent conversion of M13 to 33K-CRP in cellular extracts and a comigrating 27K cross-reactive fragment resulting from the CNBr digestion of both M13 and 33K-CRP, suggest that 33K-CRP is derived from M13.

Original languageEnglish
Pages (from-to)637-644
Number of pages8
JournalInsect Biochemistry
Issue number7
StatePublished - 1988


Acknowledgements--We would like to thank Don Kersey for his help in maintaining our insects, and Dr J. R. Fresco (Department of Biochemical Sciences, Princeton University) for his comments regarding protein fingerprinting. M. F. Minnick was supported in part by a grant from Sigma Xi.

FundersFunder number
SIGMA Clermont


    • Manduca sexta
    • epidermis
    • fat body
    • hemocyte coagulation
    • hemolymph
    • immune proteins
    • lectin
    • midgut


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