Electrophoretic properties of the globins of bovine hemoglobins A and B

Grimes, R.M.; Duncan, C.W.

doi:10.1016/0003-9861(59)90601-0

Cited by 7 publications

(4 citation statements)

References 12 publications

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“…In our studies with the buffer systems where two main bands appeared on stained starch gels (buffers 1, 2 and 3) the results agree with those of Grimes & Duncan (1959) and Muller (1961), the slower band being the a-chain and the faster the non-ac-chain. Grimes & Duncan (1959) also reported the finding ofa third component ofboth cattle globins at pH 2-4. The mobilities of the respective three components were essentially the same for both globins.…”

Section: Methodssupporting

confidence: 90%

“…The differences between the two most common adult cattle haemoglobins, HbA and HbB, has been found in electrophoretic properties of the globins (Grimes & Duncan, 1959), the total amino acid composition of the haemoglobin, however, being the same (Hojgaard, Moustgaard & Moller, 1960;Efremov, 1963). Grimes & Duncan studied the purified globins (A and B) by moving-boundary electrophoresis and found that at pH107 one of * Present address: Uiniversity of Skopje, Yugoslavia.…”

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Differences in cattle globins

Ефремов¹,

Braend²

1965

Biochemical Journal

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1. Comparisons have been made between electrophoretic mobilities of the cattle haemoglobins, HbA, HbB, HbC, HbD and HbF, at pH8.9. The fastest was HbB, then came in decreasing order HbF, HbC, HbA and HbD. 2. Globins were prepared from the main fractions of the five haemoglobins by CM-cellulose chromatography and investigated by starch-gel electrophoresis in four different buffer systems. In three of these (pH2.0 and 11.8) the globins appeared as two bands on stained starch gels. The slowest bands, the alpha-chains, showed the same rate of migration in all five globins. The faster bands, the non-alpha-chains, differed, that of HbF being the fastest and that from HbC the slowest. The other three were intermediate with, however, very small difference between the non-alpha-chains from HbA and HbD. 3. At pH1.8 in an acetate-phosphate-hydrochloric acid-urea buffer three bands appeared in all five globins of which the two slowest were indistinguishable in rates of migration, whereas the rates of migration of the third and fastest bands differed. Explanations for the occurrence of three bands are discussed.

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Section: Methodssupporting

confidence: 90%

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confidence: 99%

Differences in cattle globins

Ефремов¹,

Braend²

1965

Biochemical Journal

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“…Changes in the types of haemoglobins produced in developing organisms have also been re ported for a number of other species (Gratzer & Allison i960;Muller 1961); for example, the cyclostome (Adinolfi, Chieffi & Siniscalco 1959), the rat , the mon key, Macaca speciosa (Kitchen, Eaton & Stenger 1968), cattle, pigs and sheep (Kleihauer & Stoffler 1968;Kleihauer, Brauchle & Brandt 1966;Grimes & Duncan 1959), and goats (Adams, Wrightstone, Miller & Huisman 1969). In cattle, pigs and sheep, two embryonic haemoglobins, similar in chain composition to Gower 1 and Gower 2 of the human embryo, are progressively replaced by foetal haemoglobin, and subsequently by the adult type haemoglobin.…”

Section: (D) Heterogeneity Of Haemoglobins Other Vertebratesmentioning

confidence: 98%

The erythroid cells and haemoglobins of the chick embryo

Bruns

Ingram

1973

Phil. Trans. R. Soc. Lond. B

186

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The changes in the types of erythroid cells produced during embryogenesis of the chick have been correlated with the changes in the types of haemoglobins found in the embryo. Primitive erythroid cells constitute the only red blood cells of 2- to 5-day embryos. The first recognizable immature definitive erythroid cells appear in the embryonic circulation at 5 to 6 days and progressively replace the primitive cells, such that by 14 to 16 days the primitive cells constitute less than 1 % of the circulating erythroid cells. Primitive erythropoiesis is strikingly different from definitive erythropoiesis. At any one time point between 2 and 16 days, all of the isolated primitive cells appear, by morphological criteria, to be at the same stage of maturation, and, although variation in cell size is observed, for an individual maturation stage, the small cells are not more mature than the medium-size cells, nor are the large cells less mature than the medium or small cells. Maturing primitive erythroid cells undergo the progressive changes in cell structure characteristic of erythroid maturation in mammalian erythropoietic systems, but do so as a uniform cell population. Haemoglobin, isolated from primitive erythroid cells of 2- to 5-day embryos, shows two components on polyacrylamide gel electrophoresis, haemoglobin E and haemoglobin P. The haemoglobin E/P ratio is constant in lysates from 2- to 5-day embryos. A t 6 to 7 days when the first haemoglobinized immature definitive erythroid cells appear in the embryonic circulation, two new haemoglobin components are observed in lysates of erythroid cells. These two new haemoglobin components are electrophoretically and immunologically identical to the two haemoglobin components of adult chickens, haemoglobins A and D. As the definitive erythroid cells replace the primitive erythrocytes in the embryonic circulation, the haemoglobins A and D increase in amount and replace haemoglobin P. Haemoglobin P cannot be detected immunologically in erythroid cell lysates from 16-day embryos which contain less than 1 % primitive cells. In erythroid cell lysates from late embryos, which contained few, if any, primitive erythrocytes, a minor haemoglobin, electrophoretically similar to haemoglobin E on pH 10.3 polyacrylamide gels, is consistently observed. This component differs from haemoglobin E on pH 8.9 polyacrylmide gels, on Sephadex G-100 columns, on polyacrylamide gels of different porosities, and shows a reaction of only partial identity with haemoglobin E by two-dimensional immunodiffusion. This haemoglobin component, haemoglobin H, is detectable electrophoretically in lysates from 12-day embryos and immunologically in lysates from 8-day embryos. Haemoglobin H has not been observed in adult chickens. The switch from the production of primitive to definitive erythroid cells during development of the chick embryo is associated with the initiation of synthesis of three new haemoglobins, the two adult haemoglobins and haemoglobin H. The haemoglobin D /A ratio of adult chicken haemoglobin, determined from the ratio of gel scan peak masses, is 0.30. When haemoglobins D and A first appear in erythroid cell lysates from 6- to 7-day embryos, the haemoglobin D /A ratio is about 0.9. T he D/A ratio of lysates falls to 0.5 by 16 to 18 days, a time when 99 % of the erythroid cells of the embryo are mature definitive erythrocytes. However, the haemoglobin D /A ratio of lysates from late embryos and young chicks of 0.5 to 20 days of age is consistently greater than that of adult chicken haemoglobin. Definitive erythrocytes of chick embryos and young chicks appear to differ from definitive cells of adult chickens in at least two ways: the presence of haemoglobin H and the higher haemoglobin D/A ratio.

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“…This is true of Algerian and certain French breeds (Cabannes & Serain, 1955 a, 1957a), the Jersey, Guernsey and South Devon breeds among British cattle (Bangham, 1957), American Vella (1958)) using paper electrophoresis at pH 8-6 and 6.5 has found a third component, C, in a number of oxen, all three components having the same absorption spectra. The examination of bovine globin by free-boundary electrophoresis has given results which have a bearing on the nature of the subunits (see Grimes & Duncan, 1959). On electrophoresis of globins A and B at pH 4-3 both showed dissociation into two components; at pH 2-4 three components were observed with the same relative mobilities and in the same proportions.…”

Section: Multiple Haemoglobins 483mentioning

confidence: 99%