A case of proteinuria with analbuminuria.

1985 ◽  
Vol 31 (11) ◽  
pp. 1905-1906 ◽  
Author(s):  
T Sun ◽  
Y Lien ◽  
L Mailloux
Keyword(s):  
Diabetes Mellitus ◽  
Renal Failure ◽  
Chronic Renal Failure ◽  
Sodium Dodecyl Sulfate ◽  
Small Molecules ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Electrophoretic Pattern ◽  
Renal Tubules

Abstract A 46-year-old black man with diabetes mellitus and hypertension was hospitalized because of myocardial ischemia and chronic renal failure. The electrophoretogram for protein in urine revealed proteins only in the alpha 1, alpha 2, and beta regions. These protein fractions were identified as small molecules by sodium dodecyl sulfate/polyacrylamide gel electrophoresis. No albumin was detected in the urine. The molecular mass of albumin, the protein present in highest concentration in serum, is near the glomerular filtration threshold, and this protein is not reabsorbed by renal tubules; therefore, albumin is consistently present in proteinuric specimens. Thus this analbuminuric pattern is highly unusual. Although the mechanism of the analbuminuria in this case is not fully understood, we wished to document this extremely rare electrophoretic pattern to alert clinical chemists and pathologists of its existence.

Heterozygous Abnormal Fibrinogen Osaka III with the Replacement of γ Arginine-275 by Histidine Has an Apparently Higher Molecular Weight γ-Chain Variant

1992 ◽  
Vol 68 (05) ◽  
pp. 534-538 ◽  
Author(s):  
Nobuhiko Yoshida ◽  
Shingi Imaoka ◽  
Hajime Hirata ◽  
Michio Matsuda ◽  
Shinji Asakura
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulfate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Tetraacetic Acid ◽  
Fibrin Monomer ◽  
Sds Page ◽  
Thrombotic Tendency ◽  
Chain Variant

SummaryCongenitally abnormal fibrinogen Osaka III with the replacement of γ Arg-275 by His was found in a 38-year-old female with no bleeding or thrombotic tendency. Release of fibrinopeptide(s) by thrombin or reptilase was normal, but her thrombin or reptilase time in the absence of calcium was markedly prolonged and the polymerization of preformed fibrin monomer which was prepared by the treatment of fibrinogen with thrombin or reptilase was also markedly defective. Propositus' fibrinogen had normal crosslinking abilities of α- and γ-chains. Analysis of fibrinogen chains on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) in the system of Laemmli only revealed the presence of abnormal γ-chain with an apparently higher molecular weight, the presence of which was more clearly detected with SDS-PAGE of fibrin monomer obtained by thrombin treatment. Purified fragment D1 of fibrinogen Osaka III also seemed to contain an apparently higher molecular weight fragment D1 γ remnant on Laemmli gels, which was digested faster than the normal control by plasmin in the presence of [ethy-lenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA).

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