Baeyer‐Villiger‐Reaktion der Silylketone (I) bzw. (V) in Gegenwart von NazHPO4 ‐Puffer liefert die Lactone (II) bzw. (VI) [das instabile Lacton (VIb) ist mit dem stabilen Isomeren (IX) verunreinigt], die zu den Hydroxysilanen (III) bzw. (VII) verseift werden.
In contrast to the corresponding enolate, the metalloenamine obtained from (IV) + (II) undergoes α‐alkylation in a regio‐ and stereoselective fashion even with less reactive electrophiles such as (III) and (V), thus giving access to the desired trans‐α‐alkyl‐β‐silyl ketones (six examples given).
Human oxyhemoglobin reacts with mellitic dianhydride to produce a modified protein which shows a reduced oxygen affinity over a wide pH range, a reduced but significant cooperativity, a reduced Bohr effect and no response to the allosteric effectors: chloride, clofibric acid or inositol hexaphosphate. The amount of crosslinking in the modified hemoglobin is approximately 22% suggesting promise as a blood substitute. Reaction of deoxyhemoglobin with mellitic dianhydride produces a modified protein with reduced response to clofibric acid and a decrease in oxygen affinity in the presence of inositol hexaphosphate.
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