Structural or functional heterogeneity of normal human serum albumin, allo albumin, bisalbumin

Giuliani, Alessandro; Hammoud, Hassan; Casalbore, Patrizia; Marini, L.; Orlando, M.; Tentori, L

doi:10.1016/0009-8981(81)90438-1

Cited by 8 publications

(2 citation statements)

References 11 publications

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“…In most cases, no evidence is present of pathologic situations concomitant with bisalbuminemia. 7 Genetic variants of albumin show a migration pattern different from that of the common albumin, giving rise to the electrophoretic phenomenon of bisalbuminemia. The persistence of bisalbuminemia in our patient suggests that the condition was of genetic origin, although serum protein electrophoresis and genetic studies on the patient's family members were not available.…”

Section: Discussionmentioning

confidence: 98%

Bisalbuminemia in chronic kidney disease

et al. 2004

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Hereditary and acquired bisalbuminemia, in which the serum contains an albumin variant differing from albumin A by single amino-acid substitutions, have been reported in different races or ethnic groups and in association with various pathologic states. The importance of this rare condition in the pathophysiology of established diseases is uncertain. We evaluated a 68-year-old woman with chronic kidney disease who presented with worsened serum creatinine concentration despite lack of dietary or medical changes. Serum protein electrophoresis was performed with an automated rapid electrophoresis system. Bisalbuminemia was noted as an incidental finding on serum protein electrophoresis. The serum creatinine level stabilized with dietary protein restriction and a beta-blocking agent/diuretic combination for blood pressure control. Although the possibility that some physiologic or pharmacologic substances may not bind to abnormal albumin variants as well as they bind to normal albumin should not be discounted, the finding of bisalbuminemia did not influence the diagnosis, management, course, or prognosis of chronic kidney disease. The role of persistent bisalbuminemia in renal disease is uncertain.

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Section: Discussionmentioning

confidence: 98%

Bisalbuminemia in chronic kidney disease

et al. 2004

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“…Pencillin G is known to form covalent addition products with HSA by opening the lactame ring and acylation of amino groups in lysine side chains [4-61. As a result, the electrophoretic properties of the protein are altered [2,[7][8][9][10]. Ampicillin, a widely used derivative of penicillin G, modifies HSA with a similar mechanism [lo].…”

mentioning

confidence: 99%

Two‐dimensional electrophoresis of human serum proteins modified by ampicillin during therapeutic treatment

Magi¹,

Marzocchi²,

Bini³

et al. 1995

Electrophoresis

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Two-dimensional electrophoretograms of serum proteins from ampicillin-treated patients were analyzed-by immunoblotting with an antiserum specific for penicilloyl groups. As expected, human serum albumin (HSA) was the main ampicilloylated serum component. Transferrin main form II was found to be the second most important component as regards immunoblotting intensity. Immunoreactive spots were present on the acidic side of the transferrin isoelectric series, suggesting a modification mechanism similar to that observed in HSA, i.e., acylation of basic amino acid residues. Several additional ampicilloylated spots were detected but could not be assigned. Their electrophoretic parameters were determined using internal standards. This is the first description of serum proteins other than HSA being modified by ampicillin in the course of routine therapeutic treatment.

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