Adenosine 5′-Triphosphate-Arginine Phosphotransferase From Lobster Muscle: Purification and Properties

Virden, Richard; Watts, D C; Baldwin, Ernest

doi:10.1042/bj0940536

Cited by 75 publications

(54 citation statements)

References 13 publications

(8 reference statements)

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“…The nature of the starting material probably accounts for the comparatively low specific activity of arginine kinase in the crude extract of whole flies. This activity is up to 10 times lower than in other reported purification procedures of arthropod arginine kinase where muscle tissue alone instead of whole animals could be used [6,22,23]. A typical purification protocol is summarized in Table 2.…”

Section: Purification and Characterizationmentioning

confidence: 80%

“…This may have been caused by the high sensitivity of the enzyme towards oxidation. Since this behaviour is quite different from what is known of most of the other arthropod arginine kinases [6,22,23] we tested the stability of the enzyme by dialyzing it for 12 h in the presence and absence of sulfhydryl reagents a t different pH values ( Table 3). I n the presence of the sulfhydryl reagent the enzyme was stable a t pH values above 8.0.…”

Section: Purification and Characterizationmentioning

confidence: 99%

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Properties of Arginine Kinase from Drosophila melanogaster

Wallimann

Eppenberger

1973

European Journal of Biochemistry

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1. Starch‐gel electrophoresis of extracts of several strains of the genus Drosophila reveals neither allelic variants nor isoenzymes of arginine kinase. Arginine kinase of the drosophilid Zaprionus vittiger migrates differently. 2. Arginine kinase is non‐uniformly distributed in tissues of Drosophila melanogaster. The activity in muscle tissue represents about 70% of the total activity. A characteristic fluctuation of the enzyme activity during the development from the egg to the adult stage can be observed. 3. Purification of arginine kinase of Drosophila melanogaster has been achieved. Several physico‐chemical properties of the enzyme have been determined. The molecular weight in the range of 40 000 is comparable to other arthropod arginine kinases and suggests that the active enzyme is a monomer.

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Section: Purification and Characterizationmentioning

confidence: 80%

Section: Purification and Characterizationmentioning

confidence: 99%

Properties of Arginine Kinase from Drosophila melanogaster

Wallimann

Eppenberger

1973

European Journal of Biochemistry

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“…21 enzymes. Contradictory results were first reported : from kinetic experiments it was indicated that the reaction catalyzed by sea-crayfish arginine kinase occurred with the formation of a phosphorylated intermediate, via a "ping-pong" mechanism [5], while it was demonstrated with lobster arginine kinase that the reaction proceeded via a ternary complex between the nucleotidic substrate, the enzyme and the guanidine substrate [4].…”

Section: Mechanism Of the Reactionmentioning

confidence: 99%

“…However, additional difficulties were encountered owing to the small quantity of material available, its poor enzyme content, the numerous steps required for the purification, the low yield of the preparation and the instability of the enzyme even in the presence of protecting agents. In that respect, the enzyme differs greatly from the stable arginine kinase of Homarus vulgaris [3,4] and Palinurus longipes [22] and rather resembles the labile one from Sipunculus nudus [7]. …”

Section: Preparationmentioning

confidence: 99%

Unspecific Arginine Kinase of Molecular Weight 150 000. Purification and Properties

1971

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Arginine kinase has been purified from body-wall muscle of a marine polychaetous annelid, Sabella pavonina. The preparation is homogeneous to analytical ultracentrifugation and disc electrophoresis on polyaorylamide gel. The enzyme is labile and undergoes a rapid decrease of its specific activity, even in the presence of protecting agents. The molecular weight of the native enzyme is 150000 f 5000, the sedimentation coefficient si,,, being found to be equal to 7.5.Unlike the enzyme from lobster muscle (mol. wt -43000) and that from Sipunculus nudus muscle (mol. w t -83000), the phosphokinase from Sabella pavonina muscle is not strictly specific towards L-arginine. The enzyme shows no optical isomer specificity and is slightly active on a number of analogues of L-arginine, the integrity of the guanidine and carboxylic groups of which is indispensable to their activity. The enzyme is strictly specific for the nucleotidic substrate ATP.Partial isotopic exchange and kinetic studies suggest that the reaction mechanism is somewhat different from that described for sea-water crustacean muscle arpinine kinase and more similar to that reported for other phosphagen phosphokinases.

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“…Arginine kinase from lobster, Homarus vulgaris, was prepared as described by Virden et al (1965). The enzyme from sea cucumber, Holothuriaforskali, was purified as described by Anosike et al (1975).…”

Section: Enzymesmentioning

confidence: 99%

Effects of anions on a monomeric and a dimeric arginine kinase

Anosike

Watts

1975

Biochemical Journal

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1. Some effects of anions on the rates of phosphoarginine synthesis by monomeric (lobster) and by dimeric (Holothuria forskali) arginine kinases are reported. 2. As with creatine kinase, acetate ions activate both enzymes: C1-was also found to activate both although this was an inhibitor of creatine kinase. 3. NO3-inhibits the lobster enzyme.Inhibition is of the mixed type with respect to MgATP. K1 >K1' and K, >IK.' indicating that the presence of N03-promotes the binding of substrate and vice versa. 4. NO3-alone has no effect on the difference spectrum of the lobster enzyme but in the presence of arginine, MgATP, MgADP, MgAMP or MgIDP the difference spectrum is greatly enhanced. A profound effect on the ionization state oftyrosine residues is inferred. 5. With the Holothuria enzymelow concentrations ofNO3-activate in a manner that iscompetitive with arginine. Higher concentrations cause inhibition of the mixed type with respect to arginine in a similar manner to that found with MgATP for the lobster kinase. 6. Ofa range of anions tested only NO3-and NO2-enhanced the inhibition of enzyme activity by MgADP, indicating the formation of a pseudo-transition-state dead-end complex, enzyme-arginine-NO3-MgADP. The effect was essentially independent of temperature with the Holothuria enzyme, but with the lobster enzyme was much less marked and temperature dependent. The difference may reflect the different stabilities of the monomer and dimer enzymes, although with neither arginine kinase is the stabilization of the dead-end complex as marked as is found with creatinine kinase.Mitner-White & Watts (1971) found tha-t a strong inhibition of rabbit muscle creatine kinase was caused by NO3-ions in the presence of the dead-end complex, creatine-enzyme-MgADP. It was suggested that the planar anion acted by mimicking the transferable phosphoryl group in a transition stage in the reaction and thereby locked the two substrates together. The effectiveness of other anions as inhibitors was related to the extent to which they could behave like NO3-ions. Detailed protonrelaxation-rate studies by Cohn and co-workers confirmed and extended this hypothesis (McLaughlin & Cohn, 1972;, and recently further support has come from investigations with the fluorescent probe 8-anilinonaphthalene-1-sulphonate (McLaughlin, 1974 The work reported below was designed to discover whether arginine kinases were inhibited by low concentrations of anions, lOOmm and less, in a similar manner to the creatine kinases. With two arginine kinases, the monomeric form from the lobster, Homarus vulgaris, and the dimeric form from the sea cucumber, Holothuria forskali, evidence has been presented to indicate that stabilization of a substrate dead-end complex could occur. However, the picture is complicated by additional protein-ion interactions. Materials and MethodsADP (disodium salt) and ATP (disodium salt) were

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Adenosine 5′-Triphosphate-Arginine Phosphotransferase From Lobster Muscle: Purification and Properties

Cited by 75 publications

References 13 publications

Properties of Arginine Kinase from Drosophila melanogaster

Properties of Arginine Kinase from Drosophila melanogaster

Unspecific Arginine Kinase of Molecular Weight 150 000. Purification and Properties

Effects of anions on a monomeric and a dimeric arginine kinase

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