Multiple adenosine deaminases in the amphibia and their possible phylogenetic significance

Pang, F.; Fisher, James R.

doi:10.1016/0010-406x(68)90608-7

Cited by 30 publications

(9 citation statements)

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“…In particular, three molecular weight ranges are characteristic of the enzyme in vertebrates: type A (mol wt -200 000); type B (mol wt -I00 000); and type C (mol wt -35 000) ( Ma and Fisher, 1968, 1969,197 I . 1972).…”

Section: Characterization Of Adenosine Deaminase From Normal Colon Anmentioning

confidence: 99%

Characterization of adenosine deaminase from normal colon and colon tumors. Evidence for tumor-specific variants

Pp¹,

Me²

1978

Biochemistry

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Section: Characterization Of Adenosine Deaminase From Normal Colon Anmentioning

confidence: 99%

Characterization of adenosine deaminase from normal colon and colon tumors. Evidence for tumor-specific variants

Pp¹,

Me²

1978

Biochemistry

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“…In contrast, in many lower vertebrates, an additional, kinetically different, ADA iso zyme of 100,000 daltons (ADA2) emerges as a maj or component of total ADA activity [1,[21][22][23]. Thus, avian liver contains, in equal amounts, two ADA isozymes with molecular weights of approximately 100,000 and 35,000 daltons [1], The 100,000-dalton ADA2 iso zyme differs from the 35,000-dalton ADAi isozyme not only in molecular weight, but in kinetic properties.…”

Section: Introductionmentioning

confidence: 99%

Comparison and Possible Homology of Isozymes of Adenosine Deaminase in Aves and Humans

Ratech

Thorbecke

Meredith

et al. 1981

Enzyme

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Two kinetically distinct adenosine deaminase (ADA) isozymes with different molecular weights (35,000 and 100,000 daltons) are found in chicken liver in approximately equal amounts. The 100,000-dalton ADA has a markedly higher K(m) for adenosine and a markedly lower deaminating activity for deoxyadenosine relative to adenosine than does the 35,000-dalton ADA. A 100,000-dalton ADA isozyme has only recently been detected in mammalian tissues, where, in contrast to the chicken, it is only a trace component of total ADA activity. The human 100,000-dalton ADA isozyme, compared to the human 35,000- dalton ADA isozyme, has been reported to have a higher K(m), a lower pH optimum, and a greater resistance to inhibition by erythro-9-(2-hydroxy-2-nonyl) adenine (EHNA). The similarity in K(m)s of the 100,000-dalton ADA isozyme in man and aves led us to hypothesize that these isozymes might be descended from a common ancestor and therefore also be similar as to other kinetic parameters. We now report that the chicken 100,000-dalton ADA, like the human 100,000-dalton isozyme, has a lower pH optimum and a greater resistance to inhibition by EHNA than does the avian or human 35,000-dalton isozyme. In addition, the avian 100,000-dalton isozyme is relatively resistant to inhibition by deoxycoformycin and has a cathodal rather than an anodal electrophoretic mobility at pH 6.5. Conversely, we report that the human 100,000-dalton ADA isozyme, similar to the avian 100,000-dalton ADA, has markedly lower relative deaminating activity for deoxyadenosine than does the 35.000- dalton ADA human isozyme. Thus, despite the marked difference in the relative amounts of the 100,000- and 35,000-dalton ADA isozymes in man as compared to aves, the 100.000- dalton ADA isozymes from both species exhibit several similar kinetic properties, all of which are different from those of the 35,000-dalton ADA isozymes. We also report using a new sensitive assay, relative rates of degradation by the two chicken isozymes of several naturally occurring modified adenine nucleosides which are inhibitory to in vitro human lymphocyte proliferation.

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“…This enzyme is of special interest since much evidence supports a role in the regulation of cellular growth and differentiation [e.g., Ishii & Green (1973), Meuwissen et al (1975), and Trotta & Balis (1978)].In particular, clinical and in vitro studies strongly suggest a causal relationship between the genetically determined absence of this enzyme activity and the severe combined immunodeficiency disease, which is characterized by severe defects in cellular and humoral immunity (Dissing & Knudsen, 1972;Giblett et al, 1972;Meuwissen et al, 1975). The enzyme is of additional importance because it can also catalyze the deamination and consequent inactivation of several potent antitumor and antiviral nucleosides (Brink & LePage, 1964Schabel, 1968;Plunkett & Cohen, 1975).Several variants of ADase1 that can be distinguished on the basis of charge and/or molecular weight have been described.The cytosolic vertebrate enzyme can be classified according to three molecular weight ranges: (1) >200000 (type A); (2) ~100 000 (type B); (3) ~35 000 (type C) (Ma & Fisher, 1968. In man erythrocytes contain exclusively type C enzyme, whereas varying amounts of the type A form are generally found in other tissues (Akedo et al, 1970(Akedo et al, , 1972Edwards et al, 1971).…”

mentioning

confidence: 99%

“…The cytosolic vertebrate enzyme can be classified according to three molecular weight ranges: (1) >200000 (type A); (2) ~100 000 (type B); (3) ~35 000 (type C) (Ma & Fisher, 1968. In man erythrocytes contain exclusively type C enzyme, whereas varying amounts of the type A form are generally found in other tissues (Akedo et al, 1970(Akedo et al, , 1972Edwards et al, 1971).…”

mentioning

confidence: 99%

“…Although a high molecular weight ADase has been described and partially characterized in vertebrates other than man [e.g., Ma & Fisher (1968, Murphy et al (1969), and Piggott & Brady (1976)], no animal model for the conversion proteins has been previously reported. We present here the tissue distribution of these proteins in the rabbit and the purification and partial characterization of the rabbit kidney proteins.…”

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Rabbit adenosine deaminase conversion proteins. Purification and characterization

Pp¹,

Ra²,

Schonberg³

et al. 1979

Biochemistry

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An animal model for the adenosine deaminase (ADase) conversion proteins has been demonstrated in various rabbit tissues. These proteins bind specifically to the type C rabbit or calf ADase (Mr ~35 000) to produce a large increase in molecular weight with no significant effect on maximum velocity. Kidney displayed the greatest conversion activity, followed by ileum and lung. The latter tissues were shown to have all of their ADase present as high molecular weight enzyme and were also characterized by low specific ADase activity. The molecular weight of endogenous kidney ADase was estimated as 295 000 by gel filtration chromatography. No strict correlation between the level of specific ADase activity and quantity of either ADase or free conversion protein was observed. The kidney conversion protein was purified over 1700-fold to apparent homogeneity. Purification steps included gel filtration chromatography followed either by specific .A.denosine deaminase (EC 3.5.4.4) is a widely distributed aminohydrolase that catalyzes the irreversible hydrolysis of adenosine to inosine and ammonia. This enzyme is of special interest since much evidence supports a role in the regulation of cellular growth and differentiation [e.g., Ishii & Green (1973), Meuwissen et al. (1975), and Trotta & Balis (1978)].In particular, clinical and in vitro studies strongly suggest a causal relationship between the genetically determined absence of this enzyme activity and the severe combined immunodeficiency disease, which is characterized by severe defects in cellular and humoral immunity (Dissing & Knudsen, 1972;Giblett et al., 1972;Meuwissen et al., 1975). The enzyme is of additional importance because it can also catalyze the deamination and consequent inactivation of several potent antitumor and antiviral nucleosides (Brink & LePage, 1964Schabel, 1968;Plunkett & Cohen, 1975).Several variants of ADase1 that can be distinguished on the basis of charge and/or molecular weight have been described.The cytosolic vertebrate enzyme can be classified according to three molecular weight ranges: (1) >200000 (type A); (2) ~100 000 (type B); (3) ~35 000 (type C) (Ma & Fisher, 1968. In man erythrocytes contain exclusively type C enzyme, whereas varying amounts of the type A form are generally found in other tissues (Akedo et al., 1970(Akedo et al., , 1972Edwards et al., 1971). Proteins have been described in certain human tissues which can cause a type C to type A conversion (Nishihara et al., 1973; Schrader & Stacy, 1977;Dadonna & Kelley, 1978). These conversion proteins (Mr ~200 000) are apparently incorporated into the quaternary structure of the high molecular weight enzyme to form an oligomer fFrom the Memorial Sloan-

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Multiple adenosine deaminases in the amphibia and their possible phylogenetic significance

Cited by 30 publications

References 9 publications

Characterization of adenosine deaminase from normal colon and colon tumors. Evidence for tumor-specific variants

Characterization of adenosine deaminase from normal colon and colon tumors. Evidence for tumor-specific variants

Comparison and Possible Homology of Isozymes of Adenosine Deaminase in Aves and Humans

Rabbit adenosine deaminase conversion proteins. Purification and characterization

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