An American text-book of physiology . plaining the purplish colorof hsemoo-lobin solutions and ofvenous blood. Oxyhsemoglobiu so-lutions can be converted to hiemo-globin solutions, with a correspond-ing change in the spectrum bands,by placing the former in a vacuumor, more conveniently, by addingreducing solutions. The solutionsmost commonly used for this pur-pose are ammonium sulphide andStokess reagent.^ If a solution ofreduced hemoglobin is shaken withair, it quickly changes to oxyhsemo-globin and gives two bands insteadof one when examined through thespectroscope. Any given solutionmay be
An American text-book of physiology . plaining the purplish colorof hsemoo-lobin solutions and ofvenous blood. Oxyhsemoglobiu so-lutions can be converted to hiemo-globin solutions, with a correspond-ing change in the spectrum bands,by placing the former in a vacuumor, more conveniently, by addingreducing solutions. The solutionsmost commonly used for this pur-pose are ammonium sulphide andStokess reagent.^ If a solution ofreduced hemoglobin is shaken withair, it quickly changes to oxyhsemo-globin and gives two bands insteadof one when examined through thespectroscope. Any given solutionmay be changed in this way fromoxyhsemoglobin to hoemoglobin,and the reverse, a great numberof times, thus demonstrating thefacility with which haemoglobintakes up and surrenders oxygen. ^ Stokess reagent is an ammoniacal solution of a ferrous salt. It is made by dissolving 2parts (by weight) of ferrous sulphate, adding 3 parts of tartaric acid, and then ammonia to dis-tinct alkaline reaction. A permanent precipitate should not be aBC Fig. 91.—Diagram to show the variations in the ab-sorption spectrum of reduced hremoglobin with vary-ing concentrations of the solution (after Rollett). Thenumbers to the right give the strength of the hsemo-globin solution in percentages; the letters give the posi-tions of the Fraunhofer lines. For further directionsas to the use of the diagram, see the description ofFigure 89. 342 AN AMERICAN TEXT-BOOK OF PHYSIOLOGY. Solutions of* carbon-monoxide hnemoglobin also give a .spectrum willi twoabsorption bands closely resembling in position and appearance those of oxy-ha^nioglobin (see PI. I. spectrum 7). They are distinguislicd from tiie oxy-ha?moglobin bauds by being slightly nearer the blue eud of the spectrum, asmay be demonstrated by observing the wave-lengths or, more conveniently,by superimposing the two spectra. Moreover, solutions of carbou-mouoxidehaemoglobin are uot reduced to lueraoglobin by adding Stokess licjuid, twobands being st
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