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.
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
Sandra E
SE
Vairo Cavalli
María C
MC
Arribére
Adriana
A
Cortadi
Néstor O
NO
Caffini
Nora S
NS
Priolo
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