Amino Acid Substitutions in Albumin Variants Found in Brazil

• Published in: Proceedings of the National Academy of Sciences - PNAS 1989-03, Vol.86 (6), p.1821-1825
• Main Authors: Arai, Kunio, Huss, Karen, Madison, Jeanne, Putnam, Frank W., Salzano, Francisco M., Maria H. L. P. Franco, Santos, S. E. B., Maria J. M. Freitas
• Format: Article
• Language: English
• Subjects: albumin; Albumins; Amino Acid Sequence; Amino acid substitution; Amino acids; Biochemistry; Brazil; Chromatography, Gel; Chromatography, High Pressure Liquid; Cyanogen Bromide; Electrophoresis; Electrophoresis, Starch Gel; Gels; Genetic mutation; Genetic screening; Genetic Variation; Glutamates; Glutamic Acid; Hemoglobins, Abnormal; Humans; Lysine; Molecular genetics; Molecular Sequence Data; Peptide Fragments; point mutation; Polymorphism, Genetic; Serum Albumin - genetics; Starches; Trypsin
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.86.6.1821

Conventional horizontal starch-gel electrophoresis in four buffer systems and structural studies were performed on four albumin variants, and the findings were compared with similar previous data. Albumins Coari I and Porto Alegre I have a previously unreported amino acid substitution (glutamic acid replaced by lysine at position 358, denoted 358 Glu → Lys). The alteration in albumin Porto Alegre II (501 Glu → Lys) is the same as that found for three alloalbumins of Asiatic origin, designated Vancouver, Birmingham, and Adana. Albumin Oriximina I has the same exchange as albumin Maku (541 Lys → Glu). Some of these findings can be explained only by the occurrence of independent mutations at the same site in the albumin gene. They also point to a third cluster of mutations in that gene. indicating hypermutability in some of its segments.