A structural subunit molecular weight of urease

Reithel, F.J.; Robbins, John E.; Gorin, George

doi:10.1016/0003-9861(64)90421-7

Cited by 61 publications

(24 citation statements)

References 10 publications

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“…That these considerations may apply to proteins having partial specific volumes very different of those of the six proteins examined above appears justified by the results of Reithel et al (1964). In conditions roughly similar to ours, they find that the apparent molecular weight of ribonuclease measured in 6 M guanidine hydrochloride is identical with its real molecular weight provided one uses as 0 the value 0.700 found in dilute buffer solutions.…”

Section: B I O C H E M I S T R Ysupporting

confidence: 71%

Determination of molecular weight of proteins and protein subunits in the presence of 6M guanidine hydrochloride

Ullmann¹,

Goldberg²,

Perrin³

et al. 1968

Biochemistry

162

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For six proteins of well-established molecular structure, the apparent molecular weights have been measured in 6 M guanidine hydrochloride. It is shown that this apparent value is proportional to the G uanidine hydrochloride is now widely used as a denaturing and solubilizing agent for proteins, because of its property of abolishing noncovalent inter-and intramolecular interactions of polypeptide chains. Therefore it should be a valuable tool for determining the molecular weight of the subunits (protomers) of oligomeric proteins. However because of uncertainties regarding the partial specific volume and the degrees of hydration and solvation of proteins in the presence of high concentrations of guanidine hydrochloride, centrifugation experiments have not so far allowed molecular weight determinations in the presence of guanidine hydrochloride. However, to the extent that in the presence of guanidine hydrochloride the secondary, tertiary, and quaternary structures of proteins are completely abolished, one would presume that the relevant physical properties mentioned above should depend only on the amino acid composition of the polypeptide chain, regardless of its actual sequence. Then, for most natural polypeptides, the amino acid composition of which do not differ widely, the partial specific volume, degrees of hydration and solvation in guanidine should be practically identical. Therefore and to the extent that this assumption is correct, the ap-

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Section: B I O C H E M I S T R Ysupporting

confidence: 71%

Determination of molecular weight of proteins and protein subunits in the presence of 6M guanidine hydrochloride

Ullmann¹,

Goldberg²,

Perrin³

et al. 1968

Biochemistry

162

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“…Methods and remarks (a) Oligomeric state Sumner, Gralen & Eriksson-Sedimentation velocity and diffusion measurements Quensel (1938) Sehgal & Tanis (1965) Sucrose-density-gradient centrifugation Reithel & Robbins (1967) High-speed sedimentation equilibrium method, in dilute solution Tanis & Naylor (1968) Sucrose-density-gradient analysis Gorin, Chin & Wang (1968) Dissociation in acetate buffer; retention of enzymic activity (b) Subunit Setlow (1952) Inactivation by deuterons Reithel, Robbins & Gorin (1964) Ultracentrifugation with guanidine hydrochloride Bailey & Boulter (1969) Polyacrylamide-gel electrophoresis Tables 1, 2 and 3 summarize reports from the literature of the aggregate molecular weights of the two enzymes used and of the molecular weights of the functional subunits.…”

Section: Referencementioning

confidence: 99%

Radiation-target molecular weights of urease and of l-glutamate dehydrogenase, and their relevance to the size of the functional subunits

Blum

Alper

1971

Biochemical Journal

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Activities of the oligomeric enzymes urease and l-glutamate dehydrogenase were measured after exposure as dry preparations to various doses of electron radiation. Inactivation curves were exponential. ;Target sizes' deduced from these were small compared with the molecular weights of the whole enzyme molecules, but accorded well with independent estimates of the sizes of functional subunits. It was concluded that, when these were in associated from, there could be no transfer of absorbed energy between subunits.

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“…Later, Sehgal and co-workers (Sehgal, Tanis & Naylor, 1965;Sehgal & Naylor, 1966) also noted the 12s species and suggested that it might represent the monomeric form of the enzyme. Reithel, Robbins & Gorin (1964), using guanidine hydrochloride, determined that there were six sub-units comprising the 18s urease molecule. These sub-units of mol.…”

mentioning

confidence: 99%

Physical and chemical studies of a low-molecular-weight form of urease

Tanis

Naylor

1968

Biochemical Journal

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1. A new form of enzymically active jack-bean [Canavalia ensiformis (L.) DC] urease corresponding to an S(20,w) value of 11.8s and a molecular weight of 260000 was investigated. 2. Conversion of 18s urease (EC 3.5.1.5) into the 12s form depends on both low protein concentration and pH. Above pH5.3 urease exists in the 18s form and below pH4.8 in the 12s form; between these two pH values a 12s-18s rapid-equilibrium process is observed. 3. Comparison of the properties of 18s and 12s urease indicated no major differences. 4. A survey of other good urease sources revealed that the 12s form can also be obtained from soya bean (Glycine soja Sieb. and Zucc. cultivar Biloxi) and the bacterium Bacillus pasteurii (Miguel) Migula, but not from watermelon (Citrullus vulgaris Schrad. cultivar Congo). 5. The 12s forms from jack bean and Bacillus pasteurii did not hybridize.

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A structural subunit molecular weight of urease

Cited by 61 publications

References 10 publications

Determination of molecular weight of proteins and protein subunits in the presence of 6M guanidine hydrochloride

Determination of molecular weight of proteins and protein subunits in the presence of 6M guanidine hydrochloride

Radiation-target molecular weights of urease and of l-glutamate dehydrogenase, and their relevance to the size of the functional subunits

Physical and chemical studies of a low-molecular-weight form of urease

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