Literature summary for 4.6.1.18 extracted from

Picone, D.; Donnarumma, F.; Ferraro, G.; Russo Krauss, I.; Fagagnini, A.; Gotte, G.; Merlino, A.
Platinated oligomers of bovine pancreatic ribonuclease Structure and stability (2015), J. Inorg. Biochem., 146, 37-43 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
purified platinated monomeric enzyme, obtained upon RNase A incubation in 1:10 protein to metallodrug ratio, is crystallized at 25°C using the hanging drop vapor diffusion method	Bos taurus

Organism

Organism	UniProt	Comment	Textmining
Bos taurus	P61823	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining

Subunits

Subunits	Comment	Organism
More	the reaction between cis-diamminedichloroplatinum(II), cisplatin, a common anticancer drug, and bovine pancreatic ribonuclease, induces extensive protein aggregation, leading to the formation of one dimer, one trimer and higher oligomers whose yields depend on cisplatin/protein ratio. Structural and functional properties of the purified platinated species, together with their spontaneous dissociation and thermally induced denaturation, have been characterized. Platinated species preserve a significant, although reduced, ribonuclease activity. The high resistance of the dimers against dissociation and the different thermal unfolding profiles suggest a quaternary structure different from those of the well-known swapped dimers of RNase A	Bos taurus

Synonyms

Synonyms	Comment	Organism
RNase A	-	Bos taurus

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
65	-	T1/2 of platinated trimer	Bos taurus
66	-	T1/2 of native enzyme, platinated monomer and platinated dimer	Bos taurus

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Release 2023.1 (January 2023)