The distributions of subunit numbers and subunit sizes of enzymes: a study of the products of 100 human gene loci
- PMID: 782337
- DOI: 10.1111/j.1469-1809.1976.tb00144.x
The distributions of subunit numbers and subunit sizes of enzymes: a study of the products of 100 human gene loci
Abstract
1. A tabulation of subunit numbers and subunit sizes of a series of enzymes which have been studied electrophoretically in man is presented. The series of subunit numbers cover the isozyme products of 100 distinct gene loci. For 99 of these, estimates of subunit size are given. 2. The distribution of subunit numbers in the whole series is as follows: monomers, 28; dimers, 43; trimers, 4; tetramers, 24; octamers, 1. 3. The subunit sizes range from 13,000 to 116,000. The average subunit size for the whole series is close to 45,800. This corresponds to an average polypeptide chain length of about 425 amino acids. 4. No significant differences were found between the average subunit sizes for the separate classes of enzyme with different subunit numbers. 5. The enzymes were categorized in six different types according to the classification of the International Enzyme Commission. It was found that the oxido-reductases differed from the other types (transferases, hydrolases, lyases, isomerases, ligases) in showing a much greater proportion of multimeric enzymes. Only 1 out of 24 oxido-reductases appeared to be a monomer, whereas in the other enzyme types approximately one-third of the enzymes considered appeared to be monomers. No significant differences in subunit size were found between the various enzyme types. 6. It was found that, in general, where two or more separate gene loci are concerned in determining sets of isozymes with the same or very similar enzyme characteristics, there is a close correlation in subunit size and in most, though not all, cases the subunit numbers are the same.
Similar articles
-
Multilocus enzymes in man.Ciba Found Symp. 1979 Jun 27-29;(66):187-204. doi: 10.1002/9780470720486.ch8. Ciba Found Symp. 1979. PMID: 258167
-
Relationship between subunit size and number of rare electrophoretic alleles in human enzymes.Biochem Genet. 1978 Oct;16(9-10):971-85. doi: 10.1007/BF00483748. Biochem Genet. 1978. PMID: 743198
-
Size and stability to sodium dodecyl sulfate of alkaline phosphatases from their three established human genes.Biochim Biophys Acta. 1984 Nov 9;790(3):268-74. doi: 10.1016/0167-4838(84)90031-1. Biochim Biophys Acta. 1984. PMID: 6487640
-
Characteristics of the genetically determined allozymic forms of human serum paraoxonase/arylesterase.Drug Metab Dispos. 1991 Jan-Feb;19(1):107-12. Drug Metab Dispos. 1991. PMID: 1673383
-
Enzymes of nucleotide metabolism: the significance of subunit size and polymer size for biological function and regulatory properties.CRC Crit Rev Biochem. 1988;23(2):121-69. doi: 10.3109/10409238809088318. CRC Crit Rev Biochem. 1988. PMID: 3048887 Review.
Cited by
-
Increasing the resolution of polyacrylamide gel electrophoresis by varying the degree of gel crosslinking.Biochem Genet. 1979 Jun;17(5-6):499-516. doi: 10.1007/BF00498886. Biochem Genet. 1979. PMID: 117795
-
Detection of active heteropolymeric beta-glucuronidase in hybrids between mouse cells and human fibroblasts with beta-glucuronidase deficiency.Proc Natl Acad Sci U S A. 1977 Jul;74(7):2948-52. doi: 10.1073/pnas.74.7.2948. Proc Natl Acad Sci U S A. 1977. PMID: 268646 Free PMC article.
-
Evolution of the differential regulation of duplicate genes after polyploidization.J Mol Evol. 1979 Apr 12;12(4):267-317. doi: 10.1007/BF01732026. J Mol Evol. 1979. PMID: 448746
-
An evolving view of copy number variants.Curr Genet. 2019 Dec;65(6):1287-1295. doi: 10.1007/s00294-019-00980-0. Epub 2019 May 10. Curr Genet. 2019. PMID: 31076843 Review.
-
Genetic analysis of human lymphocyte proteins by two-dimensional gel electrophoresis: V. Genetic polymorphism of cytosol 31k polypeptide.Hum Genet. 1984;66(2-3):244-7. doi: 10.1007/BF00286610. Hum Genet. 1984. PMID: 6714982
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources