A compilation of amino acid analyses of proteins

Kirschenbaum, Donald M.

doi:10.1016/0003-2697(77)90057-4

Cited by 8 publications

(3 citation statements)

References 185 publications

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“…Proteins used to construct a standard curve (molecular weights given in parenthesis) were: ovalbumin, (47,000) aldolase, (161,000) and BSA (16) (20). Samples of the root preparation contained 101 ug of protein and the other samples were as indicated for Fig.…”

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confidence: 99%

Changes in Enzyme Regulation during Growth of Maize

Dicamelli

Bryan²

1975

Plant Physiol.

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The relative contribution of each of several forms of homoserine dehydrogenase (EC 1.1.1.3) to the total enzyme population in etiolated shoots and in roots of Zea mays L. var. earliking was examined by the use of gel filtration chromatography and disc gel electrophoresis. In enzyme preparations derived from shoots of seedlings grown for 72, 120, or 168 hours, two molecular forms, II and III, which have the same apparent molecular weight but differ in net charge, contributed 75 to 80 % of the total enzyme activity. A lower molecular weight species, form I, contributed 20 to 25 % of the activity from 72-hour shoots, but was found to decrease concomitantly with a proportional increase in activity contributed by aggregated enzyme form (s) during shoot development. Form I contributed a comparatively larger fraction of the total enzyme activitv in preparations of roots of 72-hour seedlings.The characteristic enzyme activity of different tissues was found to be the result of variations in both the amount and the properties of individual forms. Form I was consistently insensitive to inhibition by the feed-back modifier, L-threonine, but evidence is presented which indicates that the regulatory properties of form II and/or form III are systematically altered during shoot growth. The activity of the enzyme forms was also differentially stimulated by monovalent cations, K+ being the most effective activator; in all cases the potential for activation was correlated with the potential for inhibition. In contrast to these differences among the forms of the maize enzyme, all forms were shown to share a number of common characteristics. Potential factors which could influence the growth-associated changes in homoserine dehydrogenase are discussed briefly.

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confidence: 99%

Changes in Enzyme Regulation during Growth of Maize

Dicamelli

Bryan²

1975

Plant Physiol.

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“…P. berghei produced about 7 times the amount produced by B. rodhaini. The composition of amino acids p<0.05 * Average residues/mole of six types of rat haemoglobin (Kirschenbaum, 1975). t B. rodhaini 22.5% erythrocytes parasitized; P. berghei 44% erythrocytes parasitized.…”

Section: Discussionmentioning

confidence: 99%

“…The composition of the excess amino acid pool produced during 4 and 18 h of incubation by B. rodhaini and P. berghei, together with the amino acid composition of rat haemoglobin (Kirschenbaum, 1975), is shown in Table 3. Statistical analysis showed a significant concordance between the excess free amino acids produced by both B. rodhaini and P. berghei and the amino acid composition of rat haemoglobin.…”

Section: Estimation Of Individual Amino Acid Productionmentioning

confidence: 99%

METABOLISM OF BABESIA PARASITES IN VITRO. AMINO ACID PRODUCTION BY BABESIA RODHAINI COMPARED TO PLASMODIUM BERGHEI

Barry¹

1982

Aust J Exp Biol Med

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Summary.The in vitro amino acid production by Babesia rodhaini, Plasmodium berghei and uninfected rat erythrocytes was determined following 4 and 18 h of incubation in Krebs Ringer medium. Both parasites produced excess free amino acid. B. rodhaini produced up to 150 times and P. berghei up to 1,100 times as much free amino acid as parasite-free rat erythrocytes. The composition of excess amino acids produced by both parasites had a statistically significant concordance with the amino acid composition of rat haemoglobin, suggesting that haemoglobin was probably the main source of the amino acids produced by the parasites.

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Assessment of similarities of pairs and groups of proteins using transformed amino-acid-residue data

Reisner

Westwood²

1982

J Mol Evol

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Using as a primary standard a representative set of 208 proteins whose amino-acid-residue mole frequencies have been accurately established, a set of standard distributions of mole frequencies is defined for each amino acids, in terms of which percentile values for the observed mole frequencies of the amino-acid residues in any other protein can be determined. Data so transformed have a distribution much closer to Gaussian than untransformed values, and allow meaningful determinations of correlations between the amino-acid-residue compositions of two proteins as well as between pairs of amino-acid-residues within groups of proteins. Of the 153 possible pairs of amino acids (Asx and Glx are used) 39 are significantly correlated at p less than or equal to 0.01 and 22 at p less than or equal to 0.001. A percentile table is included for those wishing to use the method with programmable calculators. The transformed data for amino-acid compositions have been used to perform principal components analyses on groups of proteins in order to determine if meaningful sub-groupings (observable clusters in scatter diagrams) were detectable. Such analyses are shown for the representative set of proteins and for a group of 184 globins. With regard to the globin chains, a correlation is observed for alpha chains in the first principal component projection (PCP), (accounting for 22% of the variance) with respect to the evolutionary time-scale while beta chains show such a correlation in the first and second PCPs (22% and 18% of the variance respectively). Thus, alpha and beta chains appear to diverge from a common progenitor, similar in position to globin chains from "primitive" forms. Furthermore, globins from "primitive" forms are nearer to one another than they are to globins from the vertebrates, a finding without a priori reason, suggesting perhaps that once a chain has reached a stable relationship with its environment, strong constrains are placed on the co-existing globin chains so that they maintain appropriate interaction with one another. In addition, positions of the epsilon, gamma and delta chains are in the order: epsilon (embryonal) more primitive than gamma (foetal) more primitive than delta equal to beta (adult).

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A compilation of amino acid analyses of proteins

Cited by 8 publications

References 185 publications

Changes in Enzyme Regulation during Growth of Maize

Changes in Enzyme Regulation during Growth of Maize

METABOLISM OF BABESIA PARASITES IN VITRO. AMINO ACID PRODUCTION BY BABESIA RODHAINI COMPARED TO PLASMODIUM BERGHEI

Assessment of similarities of pairs and groups of proteins using transformed amino-acid-residue data

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