Constantes de sédimentation, caractères électrophorétiques et immunologiques de deux protéines isolées du sérum de rat: L'albumine et L'α1-macroglobuline

Boffa, G. A.; Jacquot-Armand, Y; Fine, J.M.

doi:10.1016/0304-4165(64)90090-x

Cited by 16 publications

(6 citation statements)

References 5 publications

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“…It too had an a, mobility on cellulose acetate. Sedimentation showed it to have a molecular weight of 739000 and an S20,w value of 18.1 S, Which was consistent with the 18.3 reported by Boffa et al (1964) for rat al-macroglobulin. It is not known whether this rat acc-macroglobulin is analogous to human a2-macroglobulin, since in the rat an a2macroglobulin is also present but only in pregnant (Beaton et al, 1961) or tumour-bearing rats (Menninger et al, 1970).…”

Section: Identification Ofseparated Proteinssupporting

confidence: 87%

A plasma protein fractionation procedure for use in studies of protein metabolism. Its application to the measurement of synthesis rates of two α1-glycoproteins and other serum proteins in the rat

Jeejeebhoy

Painter

1974

Biochemical Journal

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A two-step method for the separation of five different plasma proteins on a preparative scale, which is capable of being extended to allow the separation of other plasma proteins, is described. The proteins separated were fibrinogen, two alpha(1)-glycoproteins, albumin and transferrin. The alpha(1)-glycoproteins were characterized in terms of electrophoretic mobility, ultracentrifugal and immunological characteristics. By using this method, it was shown that a single sample of plasma could be fractionated to yield purified proteins in sufficient quantity to simultaneously measure the synthesis of the two alpha(1)-glycoproteins, albumin and transferrin in the rat with McFarlane's technique (McFarlane, 1963; Reeve et al., 1963; McFarlane et al., 1965).

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Section: Identification Ofseparated Proteinssupporting

confidence: 87%

A plasma protein fractionation procedure for use in studies of protein metabolism. Its application to the measurement of synthesis rates of two α1-glycoproteins and other serum proteins in the rat

Jeejeebhoy

Painter

1974

Biochemical Journal

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“…As yet, physicochemical data for rat plasma a, macroglobulin and 2 macroglobulin (Boffa et al, 1964;Jamieson et al, 1972a) have been insufficient to indicate whether the small separation obtained by electrophoresis in polyacrylamide gel results only from the difference in charge of these proteins or whether differences in size and shape also play a part. The present finding that the mol.wt.…”

Section: Discussionmentioning

confidence: 99%

“…These proteins, a, macroglobulin (Boffa et al, 1964;Fisher & Canning, 1966;Ganrot, 1968) and a2 macroglobulin (Darcy, 1955(Darcy, , 1957Weimer & Benjamin, 1965;Bogden & Gray, 1968;Heim, 1968;Menninger et al, 1969;Ganrot, 1973), differ in that the plasma concentration of a2 macroglobulin only, increases greatly as a result of injury or during inflammation. In such circumstances only relatively minor changes in the concentration of at1 macroglobulin have been observed.…”

mentioning

confidence: 99%

The α macroglobulins of rat serum

Gordon¹

1976

Biochemical Journal

107

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A three-stage method for isolation of alpha1 macroglobulin and alpha2 macroglobulin from the serum of normal and injured rats is described. The methods successively used, namely gel filtration, ultracentrifugation and chromatography on DEAE-cellulose, were chosen to minimize loss of tryptic esterase-protecting activity. The two proteins differed slightly with respect to the following properties: mol.wt., alpha1 macroglobulin 7.46 X 10(5), alpha2 macroglobulin 7.16 X 10(5); isoelectric focusing, alpha1, macroglobulin pI 4.4, alpha2 macroglobulin pI4.5. Amino acid analyses were identical, except with respect to tyrosine: alpha1 macroglobulin 3.96 +/- 0.24, alpha2 macroglobulin 3.16 +/- 0.32 mol/100 mol of total amino acids. When isolated from the serum of uninjured rats, alpha1 macroglobulin retained the capacity to bind 1.05 mol of trypsin/mol. However, if isolated from serum 2 days after injury only 0.78 mol of trypsin/mol of alpha1 macroglobulin was bound. alpha2 macroglobulin isolated from this latter serum bound on average 0.97 mol of trypsin/mol. When reduced with N-acetylcysteine, both molecules formed subunits of size corresponding to that expected for quarter molecules. When alpha2 macroglobulin was reduced with dithiothreitol, quarter molecules were again produced. alpha1 macroglobulin, however, when thus treated gave a more complex mixture, containing a component having a mol.wt. of less than 6 X 10(4). Antisera raised against the two proteins permitted estimation of the concentration of each protein in the plasmas or sera of normal and injured rats. Plasma from normal male rats contained 3.76 +/- 0.56 mg of alpha1 macroglobulin/ml (n = 33) and 0.016 +/- 0.001 mg of alpha2 macroglobulin/ml (n=33). After injury by injection of turpentine and cortisone, the concentrations in plasma were at 3 days 5.19 +/- 0.81 mg of alpha1 macroglobulin/ml (n = 12) and at 2 days 1.38 +/- 0.35 mg of alpha2 macroglobulin/ml (n = 12). Antisera to the two proteins did not cross-react with one another. The quarter molecules formed by reduction of both proteins showed increased antigenicity.

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“…Cellulose acetate electrophoresis showed that the HMW proteins contained a1 globulins. Polyacrylamide gel electrophoresis revealed that a1 macroglobulin and alB (Boffa, Jacquot-Armand & Fine, 1964) were the main components of HMW proteins.…”

Section: Assay Ofprotein Fractions Of Normal Adult Rat Serummentioning

confidence: 99%

INHIBITORY AND ANTI‐INHIBITORY FACTORS OF RAT SERUM ACTIVE ON THE G₁‐S TRANSITION OF HEPATOCYTE CELL CYCLE

Nadal

Boffa

1975

Cell Proliferation

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Rat hepatocytes are responsive to a serum factor inhibiting their progression through the cell cycle from the late G1 phase to the S phase. After fractionation of normal adult rat serum by two chromatographic steps on DEAE cellulose and sephadex gel filtration, the inhibitory activity was linked to proteins having a high electronegative charge and of apparent high molecular weight. Polyacrylamide gel electrophoretic analysis of active fraction showed that the α1 macroglobulin was its main component. Male and female baby rats were sensitive to the inhibitory factor from normal rats. Contrary to the normal adult rat serum the whole hepatectomized adult rat serum did not exhibit any inhibitory activity on the G1‐S transition. However, two components having antagonist activities: an α1 globulin and a γ globulin, were separated by chromatographic procedures from hepatectomized rat serum. The α1 globulin showed an inhibitory activity. It had an apparent molecular weight lower than that found in normal rats. Its activity was sex related: only male baby rats were responsive. The factor present in the γ globulin fraction was found to be antagonistic to the α1 globulin factor. Its occurrence after hepatectomy explains the absence of inhibitory activity in the serum of hepatectomized rats.

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Constantes de sédimentation, caractères électrophorétiques et immunologiques de deux protéines isolées du sérum de rat: L'albumine et L'α1-macroglobuline

Cited by 16 publications

References 5 publications

A plasma protein fractionation procedure for use in studies of protein metabolism. Its application to the measurement of synthesis rates of two α1-glycoproteins and other serum proteins in the rat

A plasma protein fractionation procedure for use in studies of protein metabolism. Its application to the measurement of synthesis rates of two α1-glycoproteins and other serum proteins in the rat

The α macroglobulins of rat serum

INHIBITORY AND ANTI‐INHIBITORY FACTORS OF RAT SERUM ACTIVE ON THE G₁‐S TRANSITION OF HEPATOCYTE CELL CYCLE

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Constantes de sédimentation, caractères électrophorétiques et immunologiques de deux protéines isolées du sérum de rat: L'albumine et L'α1-macroglobuline

Cited by 16 publications

References 5 publications

A plasma protein fractionation procedure for use in studies of protein metabolism. Its application to the measurement of synthesis rates of two α1-glycoproteins and other serum proteins in the rat

A plasma protein fractionation procedure for use in studies of protein metabolism. Its application to the measurement of synthesis rates of two α1-glycoproteins and other serum proteins in the rat

The α macroglobulins of rat serum

INHIBITORY AND ANTI‐INHIBITORY FACTORS OF RAT SERUM ACTIVE ON THE G1‐S TRANSITION OF HEPATOCYTE CELL CYCLE

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INHIBITORY AND ANTI‐INHIBITORY FACTORS OF RAT SERUM ACTIVE ON THE G₁‐S TRANSITION OF HEPATOCYTE CELL CYCLE