Occurrence of a blood group A-like substance in eggs of the prosobranch snailPomacea canaliculata

Summary In the eggs of the prosobranch snailsPomacea canaliculata andPomacea insularum a blood group A-like substance has been detected by anti-A from the snailsHelix pomatia, Helix aspersa andCepaea nemoralis.     

Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa

The iron-containing bacterioferritins contain the protoporphyrin IX haem group. It has been established that Escherichia coli cytochrome b1, cytochrome b557 and bacterioferritin are identical. The optical spectra at room temperature of the haem group show it to be predominantly low-spin in both the ferrous and ferric states. The nature of the axial ligands binding the haem group to the polypeptide has, however, remained unknown. Low-spin, bis-coordinate haem centres in proteins typically have a role in rapid electron transfer as redox changes at the metal ion lead to little structural rearrangement. There are only four amino acids with side-chains that have ligand field strengths sufficient to generate the low-spin state of haem, namely, histidine, lysine, methionine and cysteine. Hence there are, potentially, ten different pairs of these four ligands which could be discovered in electron transfer haemoproteins. To date only three have been established with certainty. They are bis-histidine, as in mammalian cytochrome b5, methionine-histidine, typified by cytochrome c and lysine-histidine, recently recognized by spectroscopic methods in cytochrome f. Here we report the electron paramagnetic resonance and near infrared magnetic circular dichroism spectra of the oxidized state of Ps. aeruginosa bacterioferritin which enable the axial ligands to be identified as the thioether side chains of two methionine residues, a ligation scheme not previously reported for haem in any protein.     

An incomplete anti-B agglutinin in the eggs of the prosobranch snailPila ovata

Zusammenfassung In den Eiern der SchneckePila ovata wurde ein Agglutinin aufgefunden, welches in «inkompletter» Weise mit einem Blutgruppen-B-ähnlichen Antigen von verschiedenen Erythrozyten reagiert. Agglutinations-und Agglutinationshemmtiter werden mit denen von den verwandten SchneckenPomacea urceus undPomacea canaliculata verglichen.     

A mutation of human cytochrome c enhances the intrinsic apoptotic pathway but causes only thrombocytopenia

We report the first identified mutation in the gene encoding human cytochrome c (CYCS). Glycine 41, invariant throughout eukaryotes, is substituted by serine in a family with autosomal dominant thrombocytopenia caused by dysregulated platelet formation. The mutation yields a cytochrome c variant with enhanced apoptotic activity in vitro. Notably, the family has no other phenotypic indication of abnormal apoptosis, implying that cytochrome c activity is not a critical regulator of most physiological apoptosis.