Morrenain b I, a papain-like endopeptidase from the latex of Morrenia brachystephana Griseb. (Asclepiadaceae).
A new cysteine endopeptidase (morrenain b I) has been purified and characterized from the latex of stems and petiols of Morrenia brachystephana Griseb. (Asclepiadaceae). Morrenain b I was the minor proteolytic component in the latex but showed higher specific activity than morrenain b II, which was the main active fraction. Both enzymes showed similar pH profiles and molecular masses, but kinetic parameters and N-terminal sequences were quite distinct, demonstrating that they are different enzymes instead of different forms of the same enzyme.
Vairo Cavalli
Sandra E
SE
LIPROVE, Departamento de Ciencias Biológicas, Facultad de Ciencias Exactas, Universidad Nacional de La Plata, C.C. 711, B1900AVW La Plata, Argentina. svairo@biol.unlp.edu.ar
Arribére
María C
MC
Cortadi
Adriana
A
Caffini
Néstor O
NO
Priolo
Nora S
NS
D000595:Amino Acid Sequence; D029062:Apocynaceae / Q000201:enzymology*; D003546:Cysteine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D015853:Cysteine Proteinase Inhibitors / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D007840:Latex / Q000737:chemistry; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010206:Papain / Q000737:chemistry*; D013379:Substrate Specificity; D013696:Temperature
D015853:Cysteine Proteinase Inhibitors; D007840:Latex; D003546:Cysteine Endopeptidases; C480299:morrenain b I, Morrenia brachystephana; D010206:Papain