Human erythrocyte protein L-isoaspartyl methyltransferase: Heritability of basal activity and genetic polymorphism for thermal stability

Archives of Biochemistry and Biophysics

Volumn 346, Issue 2, 1997, Pages 277-286

  David, Cynthia L ^a   Szumlanski, Carol L ^b   DeVry, Christopher G ^c   Ok Park Hah, Jeong ^d   Clarke, Steven ^c   Weinshilboum, Richard M ^b   Aswad, Dana W ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b MAYO CLINIC   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d Yeungnam University   (South Korea)

Author keywords

Isoaspartate; Polymorphism; Protein repair

Indexed keywords

PROTEIN ARGININE METHYLTRANSFERASE; PROTEIN L ISOASPARTYL METHYLTRANSFERASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CODON; DEAMINATION; ENZYME STABILITY; ERYTHROCYTE; GENETIC POLYMORPHISM; GENOTYPE; HEMOLYSATE; HUMAN; HUMAN CELL; ISOMERISM; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; SEGREGATION ANALYSIS; SINGLE STRAND CONFORMATION POLYMORPHISM; THERMOSTABILITY;

EID: 0031572828     PISSN: 00039861     EISSN: None     Source Type: Journal    
DOI: 10.1006/abbi.1997.0303     Document Type: Article

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