The Isolation and Electrophoretic Characterization of the Proteins in the Urine of Normal Subjects1

McGarry, Eleanor E.; Sehon, A.H.; Rose, B.

doi:10.1172/jci103138

Cited by 56 publications

(21 citation statements)

References 21 publications

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“…After filtration through cheesecloth the juice was adjusted to pH 10.0 with 2 N sodium hydroxide for 20 minutes to inactivate pepsin (7), neutralized to pH 7.0 to 8.0 with 2 N hydrochloric acid, and stored at -20°C.…”

Section: Methodsmentioning

confidence: 99%

An Immunologic Basis for Acquired Resistance to Oral Administration of Hog Intrinsic Factor and Vitamin B12 in Pernicious Anemia*

Lowenstein¹,

Cooper²,

Brunton³

et al. 1961

J. Clin. Invest.

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Section: Methodsmentioning

confidence: 99%

An Immunologic Basis for Acquired Resistance to Oral Administration of Hog Intrinsic Factor and Vitamin B12 in Pernicious Anemia*

Lowenstein¹,

Cooper²,

Brunton³

et al. 1961

J. Clin. Invest.

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“…In earlier studies, the amount of protein excreted in the urine in 24 hr by healthy humans at rest was estimated between 30 and 70 mg (1)(2)(3)(4)(5), although values of 100-400 mg have also been observed (6)(7)(8). Poortmans has reported that strenuous exercise causes an increase of protein excretion up to a hundred times the content present before exercise (9,10).…”

Section: Introductionmentioning

confidence: 99%

Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise

Poortmans¹,

Jeanloz²

1968

J. Clin. Invest.

135

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A B S T R A C r Urine was collected from 6 healthy male adults at rest and from 20 male adults after a marathon race (25 miles). The concentrated urines were quantitatively analyzed, by single radial immunodiffusion, for their content in 12 different plasma proteins: tryptophan-rich prealbumin, albumin, a,-acid glycoprotein, a1-antitrypsin, ceruloplasmin, haptoglobin, Gc-globulin, transferrin, hemopexin, f82-glycoprotein I, yA-globulin, and yG-globulin.Albumin, yA-globulin, and yG-globulin represent the major part of the plasma proteins detected in normal urine excreted by humans at rest (12, 0.5, and 2.5 mg respectively, out of a total excretion of 17.5 mg of plasma proteins per 24 hr). The other plasma proteins were excreted at a lower rate (< 0.4 mg/24 hr). The relative content of tryptophan-rich prealbumin, a1-antitrypsin, Gc-globulin, transferrin, and yG-globulin was lower in normal urine than in normal serum, whereas that of al-acid glycoprotein, 82-glycoprotein I, and yA-globulin was higher. The ratio of yG-globulin to yA-globulin was 4.9:1. When plotted on a logarithmic scale, no direct relationship between the molecular weight of a protein and the value of its renal clearance could be observed.

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“…Electrophoretic analyses of these proteins by a number of observers (1)(2)(3) have demonstrated the presence of components corresponding to each of the five major fractions present in serum. In general, however, the resolution of these peaks has been poor, and significant amounts of protein migrating more rapidly than albumin have been demonstrated.…”

mentioning

confidence: 99%

Physicochemical and Immunologic Studies of Gamma Globulins of Normal Human Urine*

Franklin

1959

J. Clin. Invest.

101

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Normal human urine has been shown to contain up to 150 mg. of protein in a 24 hour aliquot. Electrophoretic analyses of these proteins by a number of observers (1-3) have demonstrated the presence of components corresponding to each of the five major fractions present in serum. In general, however, the resolution of these peaks has been poor, and significant amounts of protein migrating more rapidly than albumin have been demonstrated. Immunoelectrophoretic studies of normal human urine by Grant (4) and Patte, Baldassaire and Loret (5) have revealed the presence of at least eight components which reacted with an antiserum to normal human serum and frequently gave reactions of identity with the corresponding proteins present in serum. Among the proteins identified by these observers were albumin, four a-globulins, two A-globulins and y-globulin (4).In spite of the qualitative similarities of the serum and urine proteins, quantitative differences in the relative amounts of the major fractions have been demonstrated. Thus, whereas albumin is the major protein component of serum, the globulin fractions predominate in urine (1, 3). The presence in urine of y-globulin at a relative concentration equal to and frequently greater than that in serum cannot be explained by current concepts concerning the origin of urinary proteins by a process of glomerular filtration of serum proteins (6, 7) followed by a nonselective tubular reabsorption (8). Such a mechanism would lead to a preferential excretion in the urine of proteins of low molecular weight and would result in an increase in their concentration relative to that of the larger proteins. Since the molecular weight of the major fraction of y-globulin in serum is approximately two and one-half times that of albumin, the presence in urine of relatively greater amounts of protein with the mobility of y-globulin suggested the existence of additional protein species which have not been detected in serum. The present study presents evidence for the existence in normal urine of proteins with a mobility similar to y-globulin and an approximate molecular weight of 35,000, and which are antigenically closely related to the y-globulin fraction of serum. While this work was in progress, low molecular weight y-globulin fractions have also been demonstrated in normal human urine by Webb, Rose and Sehon (9). MATERIAL AND METHODSTwenty-four hour urines were collected from 12 normal males and stored in the cold at 4°C. Following filtration to remove formed elements and insoluble precipitates, the urines were dialyzed against running tap water for 24 hours in the cold and concentrated to a volume of 10 to 15 ml. by pervaporation at 0 to 40 C. In a number of instances protein was precipitated by the addition of 650 Gm. ammonium sulfate to each liter of urine. Following centrifugation at 3,000 rpm for one hour, the precipitate was dialyzed against running tap water to remove the salt, and the protein solution was concentrated as above. Both methods yielded similar results. For large scale ...

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The Isolation and Electrophoretic Characterization of the Proteins in the Urine of Normal Subjects1

Cited by 56 publications

References 21 publications

An Immunologic Basis for Acquired Resistance to Oral Administration of Hog Intrinsic Factor and Vitamin B12 in Pernicious Anemia*

An Immunologic Basis for Acquired Resistance to Oral Administration of Hog Intrinsic Factor and Vitamin B12 in Pernicious Anemia*

Quantitative immunological determination of 12 plasma proteins excreted in human urine collected before and after exercise

Physicochemical and Immunologic Studies of Gamma Globulins of Normal Human Urine*

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