In Search of Holmes from Within

What appears here is part of a longer psychological study of Holmes which takes as points of focus, or rather of entree, four of his life choices: his enlistment in the Union forces while still in college in 1861, his entrance into law school in 1864, his decision to give up a law professorship at Harvard in 1882 in favor of the Massachusetts bench, and finally, his move to Washington and the Supreme Court in 1902. In a sense this last was not a choice. There were not the clear alternatives before him as there were in the first three--he was more chosen than chooser. Still, it had all the consequences and feeling of a life choice--the tearing away from the old,the embarking on the new--and, as I read the event, it was the product of his other choices, the assault on the summit of a mountain which at each point in his life Holmes committed himself to climb. And, of course, even a chosen man can choose to say no. In these pages I have used Holmes\u27s enlistment as a focus for his entire Civil War experience, thereby hoping to reveal what Holmes brought into the war and what he brought out of it. We will, I think, find in this experience the sources of Holmes\u27s world-view, of those attitudes and feelings that come to dominate his life

THE ISOLATION OF LYSOSOMES FROM EHRLICH ASCITES TUMOR CELLS FOLLOWING PRETREATMENT OF MICE WITH TRITON WR-1339

A method is described for obtaining highly purified lysosomes from Ehrlich ascites tumo cells grown in mice injected with Triton WR-1339. The isolated particles show a high specific activity for aryl sulfatase, representing an 80–90-fold purification over the homogenate, and a 15–18% yield of the total enzyme activity. Mitochondrial and microsomal marker enzymes are present in negligible amounts (0.2% of the activity of the homogenate). The biochemical evidence for a rather high degree of homogeneity of the fraction is supported by the electron microscopic examination of the purified lysosomes. The intracellular localizations of N-acetyl-β-glucosaminidase, NADH-cytochrome c reductase and NADPH-cytochrome c reductase in Ehrlich ascites cells are also reported, the first two being present in highest concentration in the combined mitochondrial-lysosomal fraction and the third in the microsomal fraction

2,6,6-Trimethyl­cyclo­hexene-1-carbaldehyde oxime

In the crystal of the title compound C10H17NO, synthesized by the reaction of β-cyclo­citral with hydroxyl­amine hydro­chloride, inversion-related mol­ecules are linked by a pair of O—H⋯N hydrogen-bonding inter­actions between the oxime functionalities, forming R 2 2(6) loops. The molecular conformation is stabilized by intra­molecular methyl C—H⋯N inter­actions. The cyclohexene ring has the typical half-chair conformation

Analysis of glycoprotein processing in the endoplasmic reticulum using synthetic oligosaccharides

Protein quality control (QC) in the endoplasmic reticulum (ER) comprises many steps, including folding and transport of nascent proteins as well as degradation of misfolded proteins. Recent studies have revealed that high-mannose-type glycans play a pivotal role in the QC process. To gain knowledge about the molecular basis of this process with well-defined homogeneous compounds, we achieved a convergent synthesis of high-mannose-type glycans and their functionalized derivatives. We focused on analyses of UDP-Glc: glycoprotein glucosyltransferase (UGGT) and ER Glucosidase II, which play crucial roles in glycoprotein QC; however, their specificities remain unclear. In addition, we established an in vitro assay system mimicking the in vivo condition which is highly crowded because of the presence of various biomacromolecules

Purification of rat-liver [gamma]-hydroxyglutamate transminase and its probable identity with glutamate-aspartate transminase

1. 1. An enzyme which catalyzes the transamination of [gamma]-hydroxyglutamate has been purified over 300-fold from rat-liver homogenates.2. 2. The following observations strongly suggest that [gamma]-hydroxyglutamate transminase is identical with glutamate-aspartate transaminase (-aspartate: 2-oxo-glutarate aminotransferase, EC 2.6.1.1): a, at all stages of purification from either rat-liver or pig-heart extracts, the glutamate to [gamma]-hydroxyglutamate transminase ratios are not significantly different; b, transaminase activity for both substrates declines at the same rate during controlled heat denaturation of the purified rat-liver enzyme; c, transamination of [gamma]-hydroxyglutamate is strongly inhibited by either -glutamate or -aspartate; d, glutarate and maleate function as competitive inhibitors for either glutamate or [gamma]-hydroxyglutamate and determined K1 values for a given inhibitor are the same for either amino acid; and e, the purified rat-liver enzyme has the same pH-activity curve for both substrates.3. 3. The erythro- and threo-isomers of [gamma]-hydroxy--glutamate serve as substrates for both isozymes of the rat-liver enzyme as well as for the pig-heart enzyme, although the former isomer is a somewhat better substrate. The corresponding -diastereo-isomers are enzymically inactive.4. 4. With [gamma]-hydroxyglutamate, only [alpha]-ketoglutarate and oxaloacetate serve as amino group acceptors; pyruvate, [alpha]-ketobutyrate, and [beta]-phenylpyruvate are inactive.5. 5. Other [gamma]-substituted forms of glutamic acid, including [gamma]-methyleneglutamic acid and [gamma]-hydroxy-[gamma]-methylglutamic acid, are also active with the purified enzymes.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/32138/1/0000191.pd