Generation of [Ala1,Thr6]bradykinin in the plasma of a snake, the reticulated python.
Incubation of heat-denatured plasma from the reticulated python, Python reticulatus with trypsin generated bradykinin-like immunoreactivity which was detected by radioimmunoassay using an antiserum raised against mammalian bradykinin. The primary structure of python bradykinin was established as Ala-Pro-Pro-Gly-Phe-Thr-Pro-Phe-Arg. This amino acid sequence contains two substitutions (Arg1-->Ala and Ser6-->Thr) compared with mammalian bradykinin. Treatment of python plasma with glass beads under conditions previously shown to generate [Thr6]bradykinin in the plasma of a turtle and an alligator did not generate bradykinin-like immunoreactivity. The data indicate that the plasma of a lepidosaur contains a kininogen but, unlike the plasma of chelonians and crocodilians, does not contain a prekallikrein activator related to Factor XII.
Conlon
J M
JM
Department of Biomedical Sciences, Creighton University School of Medicine, Omaha, Nebraska 68178.
Lance
V A
VA
D000595:Amino Acid Sequence; D000818:Animals; D017821:Boidae / Q000097:blood*; D001920:Bradykinin / Q000031:analogs & derivatives* / Q000097:blood* / Q000302:isolation & purification; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D005260:Female; D008969:Molecular Sequence Data; D011288:Prekallikrein / Q000378:metabolism; D011489:Protein Denaturation; D011863:Radioimmunoassay; D014357:Trypsin / Q000494:pharmacology
C089522:bradykinin, Ala(1)-Thr(6)-; D011288:Prekallikrein; D014357:Trypsin; D001920:Bradykinin