Prophenoloxidase activation in the hemolymph of American cockroach, Periplanata americana.
Prophenoloxidase has been successfully extracted in a stable condition from the Hemocytes of Periplaneta americana using cane sugar saline solution. Other media used to extract prophenoloxidase were found not suitable. Among the activators used (trypsin, chymotrypsin, sodium oleate and SDS), trypsin activated the proenzyme maximum. Activation during electrophoresis resulted in the dissociation of proenzyme in to two sub-units. The enzyme has also been localised by the agarose gel electrophoresis. The proenzyme was stable up to 50 degrees C and precipitated at 60 degrees C and above. The activated enzyme showed maximum activity at pH 7.0. Preliminary attempt has also been made to precipitate the enzyme protein against the antibody raised in rabbit.
Thangaraj
T
T
Department of Zoology, Konguandu Arts and Science College, Coimbatore, India.
Subramanium
S
S
Vinayakam
A
A
Aruchami
M
M
D000818:Animals; D004156:Catechol Oxidase / Q000378:metabolism*; D002850:Chromatography, Gel; D004587:Electrophoresis, Agar Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation / Q000502:physiology; D004792:Enzyme Precursors / Q000378:metabolism*; D004795:Enzyme Stability / Q000502:physiology; D006458:Hemolymph / Q000201:enzymology*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D005779:Immunodiffusion; D010526:Periplaneta / Q000201:enzymology*; D012965:Sodium Chloride
D004792:Enzyme Precursors; D012965:Sodium Chloride; C038451:pro-phenoloxidase; D004156:Catechol Oxidase