T.H.J. Huisman, J.M.Schillhorn Van Veen, A.M. Dozy, C.M. Nechtman
{"title":"动物血红蛋白的研究2。无机磷酸盐对成年鸡血红蛋白理化生理特性的影响","authors":"T.H.J. Huisman, J.M.Schillhorn Van Veen, A.M. Dozy, C.M. Nechtman","doi":"10.1016/0926-6577(64)90190-1","DOIUrl":null,"url":null,"abstract":"<div><p>The equilibrium of dilute and concentrated adult chicken red blood cell hemolysates with O<sub>2</sub> has been studied using potassium phosphate buffers and NaCl solutions of different molarities. The results indicate an increase in O<sub>2</sub> affinity with increase in ionic strength. The same phenomenon was observed for the isolated minor hemoglobin component; the isolated major hemoglobin component showed a rather high O<sub>2</sub> affinity at low ionic strength, which decreased with increase in molarity. The minor hemoglobin fraction exhibited an ability to form rather stable complexes with phosphate ions; such complexes possessed a high O<sub>2</sub> affinity at low ionic strength. The data also indicated that the two hemoglobin components in a hemolysate interacted with each other. This extra-molecular interaction interfered with the physiologic properties of the hemolysate. No physico-chemical interaction could be detected, as was demonstrated by the determination of the molecular weight and by viscosity measurements.</p></div>","PeriodicalId":100169,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"1964-09-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6577(64)90190-1","citationCount":"20","resultStr":"{\"title\":\"Studies on animal hemoglobins II. The influence of inorganic phosphate on the physico-chemical and physiological properties of the hemoglobin of the adult chicken\",\"authors\":\"T.H.J. Huisman, J.M.Schillhorn Van Veen, A.M. Dozy, C.M. Nechtman\",\"doi\":\"10.1016/0926-6577(64)90190-1\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The equilibrium of dilute and concentrated adult chicken red blood cell hemolysates with O<sub>2</sub> has been studied using potassium phosphate buffers and NaCl solutions of different molarities. The results indicate an increase in O<sub>2</sub> affinity with increase in ionic strength. The same phenomenon was observed for the isolated minor hemoglobin component; the isolated major hemoglobin component showed a rather high O<sub>2</sub> affinity at low ionic strength, which decreased with increase in molarity. The minor hemoglobin fraction exhibited an ability to form rather stable complexes with phosphate ions; such complexes possessed a high O<sub>2</sub> affinity at low ionic strength. The data also indicated that the two hemoglobin components in a hemolysate interacted with each other. This extra-molecular interaction interfered with the physiologic properties of the hemolysate. No physico-chemical interaction could be detected, as was demonstrated by the determination of the molecular weight and by viscosity measurements.</p></div>\",\"PeriodicalId\":100169,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-09-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6577(64)90190-1\",\"citationCount\":\"20\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926657764901901\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926657764901901","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Studies on animal hemoglobins II. The influence of inorganic phosphate on the physico-chemical and physiological properties of the hemoglobin of the adult chicken
The equilibrium of dilute and concentrated adult chicken red blood cell hemolysates with O2 has been studied using potassium phosphate buffers and NaCl solutions of different molarities. The results indicate an increase in O2 affinity with increase in ionic strength. The same phenomenon was observed for the isolated minor hemoglobin component; the isolated major hemoglobin component showed a rather high O2 affinity at low ionic strength, which decreased with increase in molarity. The minor hemoglobin fraction exhibited an ability to form rather stable complexes with phosphate ions; such complexes possessed a high O2 affinity at low ionic strength. The data also indicated that the two hemoglobin components in a hemolysate interacted with each other. This extra-molecular interaction interfered with the physiologic properties of the hemolysate. No physico-chemical interaction could be detected, as was demonstrated by the determination of the molecular weight and by viscosity measurements.