Biomedical subjects
W G Miller
Publications and source records attributed to W G Miller.
Effect of freezing on cholesterol in individual sera.
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DNA from diverse sources manifests cryptic low-level transcription in Escherichia coli.
We present evidence that DNA from diverse prokaryotic and eukaryotic sources gives rise to low-level fusion expression in Escherichia coli promoter-probe vectors. This expression may be as high as approximately 10% of the E. coli lacUV5 promoter. Although expression does not correlate with the presence of obvious E. coli promoter-like sequences, it is blocked by transcriptional terminators. Furthermore, transcription across the fusion junction is detected at levels that correlate with fusion expression. We suggest that this 'low-level transcription' (LLT) results from infrequent initiation by RNA polymerase at random sites and/or weak promoters. We propose that LLT has biological significance. In some instances, it may provide an advantageous basal level of gene expression, and we suggest that this may be true for the E. coli lacY gene. In other instances, LLT may be detrimental, in which case it may be blocked by mechanisms such as RNA secondary structure or transcriptional polarity. We present evidence to show that activation of the IS10 transposase gene by LLT is blocked at the translational level.
Determination of magnesium in serum by the technicon SMAC with a calmagite method with blank correction.
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Pooled serum products and proficiency testing.
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On the design of clinical chemistry quality-control sera.
Quality-control specimens having quantitave interspecimen relationships were prepared by (a) making admixtures of two serum pools and (b) making various dilutions of the admixtures. The specimens were analyzed for many constituents to illustrate how the data obtained could be manipulated and used. The inter-related specimens permit the reduction of quality-control data to a few target values and should be particularly useful for the evaluation of multi-channel analyzers, and for use in inter-laboratory proficiency surveys. Aspects of the design of quality control and proficiency test specimens are also discussed.
Electron transport by C-type cytochromes. I. The reaction of horse heart cytochrome c with anionic reductants.
The kinetics of reduction of horse heartcytochrome c have been investigated using the reductants sodium dithionite and potassium ferrocyanide. Sodium dithionite reduction at pH 7.0 yields rate constants of 2.8 X 10(8)M(-1)sec-1 for SO2 AND 6 X 10(5) M-1 sec-1 for S2O4 at infinite dilution. Moreover, the data presented demonstrates the participation of positively charged amino acid side chains at the site of electron transfer. The effect of pH on the reduction of ferricytochrome c requires a minimum of two pK values for description (pK1 = 7.0 +/- 0.4, pK2 = 9.3 +/- 0.3). Based on the pK values determined, one or more lysines and a residues(s) with a low pK are implicated as the positively charged residues participating in electron transfer. From a comparison of the rates of reduction of various denatured forms of cytochrome c we feel that the most viable conclusion is that electron transfer takes place at the exposed heme edge in the vicinity of the amino acid side chains indicated above. Ferrocyanide reduction of ferri-horse heart cytochrome c takes place in a kinetically complex manner. A mechanism is described which includes complexes of ferrocyanide and ferricytochrome c and ferricyanide and ferrocytochrome c. As was found for dithionite reduction a positively charged region of the cytochrome c participates in electron transfer. Combining our results with ferrocyanide and dithionite we conclude that avaible data is compatible with a single mechanism of electron transfer. It is suggested that the kinetic distinction between different reductants lies in the lifetime of the transient complex formed, with the order ferrocyanide greater than S2O4 greater than SO2.
Thermodynamic parameters of the helix-coil transition in polypeptide chains. III. Random copolymers of L-leucine and L-glutamic acid.
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