@article {94,
	title = {Analysis of fatal blunt trauma presenting at an areawide trauma center.},
	journal = {IMJ Ill Med J},
	volume = {148},
	year = {1975},
	month = {1975 Nov},
	pages = {511-5},
	keywords = {Accidents, Traffic, Adolescent, Adult, Aged, Child, Preschool, Emergency Medical Services, Female, Humans, Illinois, Male, Middle Aged, Trauma Centers, Wounds, Nonpenetrating},
	author = {Bartley, V H}
}
@article {97,
	title = {Studies on variant glucose-6-phosphate dehydrogenases: G6PD Fort Worth.},
	journal = {Biochem Med},
	volume = {13},
	year = {1975},
	month = {1975 Jul},
	pages = {264-75},
	keywords = {Adult, Drug Stability, Erythrocytes, Female, Genetic Variation, Glucosephosphate Dehydrogenase, Humans, Hydrogen-Ion Concentration, Kinetics, Male, Temperature, Texas},
	issn = {0006-2944},
	author = {Mills, G C and Alperin, J B and Trimmer, K B}
}
@article {102,
	title = {Formate assay in body fluids: application in methanol poisoning.},
	journal = {Biochem Med},
	volume = {13},
	year = {1975},
	month = {1975 Jun},
	pages = {117-26},
	keywords = {Aldehyde Oxidoreductases, Animals, Body Fluids, Carbon Dioxide, Formates, Haplorhini, Humans, Hydrogen-Ion Concentration, Kinetics, Methanol, Methods, Pseudomonas},
	issn = {0006-2944},
	author = {Makar, A B and McMartin, K E and Palese, M and Tephly, T R}
}
@article {103,
	title = {Peptide-binding macromolecules in the blood of seriously ill or mentally retarded patients.},
	journal = {J Lab Clin Med},
	volume = {87},
	year = {1976},
	month = {1976 Feb},
	pages = {299-319},
	abstract = {<p>This report describes macromolecules that bind (des-aspartic acid1)-angiotensin II, the des aspartic acid1 derivative of angiotensin I, and several biologically active and inactive analogues of these polypeptides. The macromolecules were found in the plasma of approximately 2 per cent of ambulatory adults and hospitalized children and 32 per cent of the patients at two institutions for the mentally retarded. The binding properties of these macromolecules were studied by incubating with peptides labeled with 125iodine, and separating bound from free labeled peptide using small gel filtration columns. The peptide-binding macromolecules from several patients were compared. They showed very similar specificity for a group of arginyl peptides of the des-aspartyl1-angiotensin sequence. The plasma binders differed from one another in their optimum pH and their mobility in electrophoretic fields. Those with more acid pH optima displayed more rapid electrophoretic mobility. The binders fell into two classes based on apparent molecular weight, approximately 140,000 and 250,000. Those with the higher apparent molecular weight contained a large proportion of binder that could be precipitated with antiserum to human IgA. Kinetic measurements showed that the plasma binders were somewhat heterogeneous with respect to affinity for (des-asp1)-angiotensin, with apparent association constants ranging from 10(7) to 10(8) M-1. Binding activity was labile to heat, and to treatment with pepsin or trypsin. It was inhibited by calcium, protamine, streptomycin, and some other cationic compounds. The plasma peptide binder differed in specificity and molecular weight from soluble angiotensin-binding molecules extracted from tissues, and from properties expected of a receptor for angiotensin. These macromolecules may be useful reagents for measuring (des-asp1)-angiotensins. Their presence in plasma samples may interfere with angiotensin assays in some circumstances.</p>},
	keywords = {Angiotensin II, Chromatography, Gel, Electrophoresis, Starch Gel, Humans, Hydrogen-Ion Concentration, Intellectual Disability, Kidney Failure, Chronic, Kinetics, Macromolecular Substances, Neoplasms, Osmolar Concentration, Peptides, Protein Binding, Saralasin},
	issn = {0022-2143},
	author = {Goodfriend, T L and Sindel, M and Fyhrquist, F and Hong, R and Azen, E and Stewart, J M}
}
