Updated biblio

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author = {Speeth, Sheridan Dauster}, author = {Speeth, Sheridan Dauster},
year = {1961}, year = {1961},
pages = {909} pages = {909}
},
@article{schmoldt_digitoxin_1975,
title = {Digitoxin metabolism by rat liver microsomes},
volume = {24},
issn = {0006-2952},
url = {http://www.ncbi.nlm.nih.gov/pubmed/10},
number = {17},
journal = {Biochemical pharmacology},
author = {Schmoldt, A and Benthe, H F and Haberland, G},
month = sep,
year = {1975},
note = {{PMID:} 10},
keywords = {Animals, Chromatography, Thin Layer, Digitoxigenin, Digitoxin, Hydroxylation, Male, Microsomes, Liver, {NADP}, Rats, Time Factors},
pages = {1639--1641}
},
@article{makar_formate_1975,
title = {Formate assay in body fluids: application in methanol poisoning},
volume = {13},
issn = {0006-2944},
shorttitle = {Formate assay in body fluids},
url = {http://www.ncbi.nlm.nih.gov/pubmed/1},
number = {2},
journal = {Biochemical medicine},
author = {Makar, A B and {McMartin}, K E and Palese, M and Tephly, T R},
month = jun,
year = {1975},
note = {{PMID:} 1},
keywords = {Aldehyde Oxidoreductases, Animals, Body Fluids, Carbon Dioxide, Formates, Haplorhini, Humans, Hydrogen-Ion Concentration, Kinetics, Methanol, Methods, Pseudomonas},
pages = {117--126}
},
@article{makar_formate_1975-1,
title = {Formate assay in body fluids: application in methanol poisoning},
volume = {13},
issn = {0006-2944},
shorttitle = {Formate assay in body fluids},
url = {http://www.ncbi.nlm.nih.gov/pubmed/1},
number = {2},
journal = {Biochemical medicine},
author = {Makar, A B and {McMartin}, K E and Palese, M and Tephly, T R},
month = jun,
year = {1975},
note = {{PMID:} 1},
keywords = {Aldehyde Oxidoreductases, Animals, Body Fluids, Carbon Dioxide, Formates, Haplorhini, Humans, Hydrogen-Ion Concentration, Kinetics, Methanol, Methods, Pseudomonas},
pages = {117--126}
},
@article{duggleby_competitive_1975,
title = {A competitive labeling method for the determination of the chemical properties of solitary functional groups in proteins},
volume = {14},
issn = {0006-2960},
url = {http://www.ncbi.nlm.nih.gov/pubmed/42},
abstract = {The properties of the functional groups in a protein can be used as built-in-probes of the structure of the protein. We have developed a general procedure whereby the ionization constant and chemical reactivity of solitary functional groups in proteins may be determined. The method may be applied to the side chain of histidine, tyrosine, lysine, and cysteine, as well as to the amino terminus of the protein. The method, which is an extension of the competitive labeling technique using {[3H]-} and {[14C]1-fluoro-2},4-dinitrobenzene {(N2ph-F)} in a double-labeling procedure, is rapid and sensitive. Advantage is taken of the fact that after acid hydrolysis of a dinitrophenylated protein, a derivative is obtained which must be derived from a unique position in the protein. The method has been applied to the solitary histidine residue of lysozyme, alpha-lytic protease, and Streptomyces griseus {(S.G.)} trypsin, as well as to the amino terminus of the latter protein. The following parameters were obtained for reaction with N2ph-F at 20 degrees C in 0.1 N {KCl:} the histidine of hen egg-white lysozyme, {pKa} of 6.4 and second-order velocity constant of 0.188 M-1 min-1; the histidine of alpha-lytic protease, {pKa} of 6.5 and second-order velocity constant of 0.0235 M-1 min-1; the histidine of {S.G.} trypsin, {pKa} of 6.5 and second-order velocity constant of 0.0328 M-1 min-1; the valyl amino terminus of {S.G.} trypsin, {pKa} of 8.1 and second-order velocity constant of 0.403 M-1 min-1. In addition, the results obtained provide clues as to the microenvironments of these functional groups, and indicate that the proteins studied undergo {pH-dependent} conformational changes which affect the microenvironment, and hence the chemical reactivity of these groups.},
number = {23},
journal = {Biochemistry},
author = {Duggleby, R G and Kaplan, H},
month = nov,
year = {1975},
note = {{PMID:} 42},
keywords = {Binding Sites, Binding, Competitive, Dinitrofluorobenzene, Histidine, Hydrogen-Ion Concentration, Kinetics, Muramidase, Peptide Hydrolases, Protein Binding, Streptomyces griseus, Trypsin, Valine},
pages = {5168--5175}
},
@book{isenberg_science_1992,
address = {New York},
title = {The science of soap films and soap bubbles},
isbn = {0486269604 9780486269603},
publisher = {Dover Publications},
author = {Isenberg, Cyril},
year = {1992}
} }