We performed molecular cloning of the cDNAs that encode dog and rat pancreatic phospholipases A2 to predict the primary structures of these enzymes. The deduced amino acid sequences exhibited a highly conservative feature which is common to a group of pancreatic phospholipases A2 from various animal species. Furthermore, the structures of the signal sequences of dog and rat pancreatic phospholipases A2 were predicted, although the assignment of the positions cleaved post-translationally is only tentative at the present time.
Triostin A, a cyclic octadepsipeptide, was synthesized with Z–d-Ser[Boc–Ala–MeCys(Bzl)–MeVal]–OH and Z–d-Ser[H–Ala–MeCy(Bzl)–MeVal]–OTce as key intermediates. The synthetic antibiotic was compared with natural triostin A in terms of chromatographic behaviors, NMR spectra, and antimicrobial activity to establish their identity. The NMR data on S,S′-dibenzyldihydrotriostin A showed that this intermediate lacking the disulfide linkage also existed as two conformers in chloroform. This observation excludes the possibility that the conformer equilibrium known to occur with triostin A is a consequence of the reversed chirality of the disulfide bond.
Atrophic kidney at the end-stage of renal failure and under dialysis have lesions of ACDK that might predispose to RCC in dialysis and transplant patients.
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