<b>The Polymerization of Bovine Pancreas Carboxypeptidase A</b>

Bethune, J. L.

doi:10.1021/ja00907a042

Cited by 3 publications

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“…Ay have previously employed 2 m NaCI as the upper limit of salt concentration, and 28 mg/ml was the maximum amount of protein which could be dissolved under these conditions. It has been reported briefly that approximately 45 mg/ml of enzyme may be dissolved in 2.5 m NaCI (Bethune, 1963). Two boundaries arc seen on sedimentation of the system at such higher enzyme concentrations.…”

Section: Studies Of the Solubility Of Native Carboxypeptidasementioning

confidence: 99%

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The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride^*

Bethune¹

1965

Biochemistry

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Section: Studies Of the Solubility Of Native Carboxypeptidasementioning

confidence: 99%

“…L. (1964), 6th Intern. nder appropriate conditions three proteolytic enzymes, mercuripapain (Smith et al, 1954), chymotrypsin (Massey et al., 1955;Nichol and Bethune, 1963), and carboxypeptidase A (Bethune, 1963), manifest bimodal boundary formation in the ultracentrifuge, reflecting a rapidly equilibrating polymerization (Gilbert, 1955(Gilbert, , 1959.…”

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The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride^*

Bethune¹

1965

Biochemistry

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“…From their reported Soret coefficient data, S* values for aqueous KC1 and NaC1 at 25 ~ were computed, de Bethune (12) showed that these S*'s can be well fitted from 0 to 4 molal by a four-constant equation analogous to the FUoss-Onsager (20) conductance equation S* = A ~-Bm'/2 ~-Cm -k Dm log m [13] The least squares values for the constants are listed in Table I and fit the data almost everywhere within better than _0.1 eu. The four constant equation can therefore be used to calculate S* at infinite dilution and at 0.1 molal where no direct experimental data are available.…”

Section: Reference Values For Salt Transport Entropies Potassium and mentioning

confidence: 99%

“…To extend these values to other concentrations, use was made of the postulate that 7(C1-) = J-(K +) = 89 Values of C and C* for H +, CI-, K +, Na +, Li +, and 89 + + based on these postulates are given in lines [8][9][10][11][12][13][14][15][16][17][18][19]. In lines 20 and 21, the heat capacity of water, 18 eu, is added to the H + values for C and C to convert them to the H30 + basis.…”

Section: Moving Heat Capacity Of Chloride Ion and Relatedmentioning

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The Thermal Temperature Coefficient of the Calomel Electrode Potential Between 0° and 70°C

Bethune¹,

Daley²

1969

J. Electrochem. Soc.

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The initial thermal temperature coefficient of the calomel electrode reported in Part I is combined with the results of thermal diffusion studies elsewhere to yield information about: the entropy of transport S* of the aqueous electrolytes KCI, NaCI, LiCI, HCI, and CaCI2; the experimentally determinable moving (transported)entropy S of the ion constituents CI-, K +, Na +, Li +, H +, and Ca + +. A four-constant equation analogous to the Fuoss-Onsager conductance equation is developed for the concentration dependence of the entropy of transport S* and is applied to the salts KCI and NaCI. The division of the moving entropy S into its nonmeasurable ionic component terms: the ionic transport entropy S* and the stationary entropy S, is attempted via two postulates: the Agar postulate and the KCl-bridge postulate which give results mutually consistent within about 0.8 eu (35 ~VF/deg), e.g., S~ (H +) = --5.22 eu from our data under the Agar postulate, and --4.42 eu under the KCl-bridge postulate. These values are in good agreement with previously reported values of --4.48, --5.5, and --5.7 based on a number of alternative postulates. Values are also obtained for the transport heat capacity C* of the electrolytes and for the measurable moving heat capacity C of the --4 ion constituents at 30 ~ A division of C into its nonmeasurable ionic components: C* and C is also carried out on the basis of Fales and Mudge's hydrogen thermal emf data via the KCl-bridge posUllate, and yields, e.g., C*o ----30 eu (Cl-), 5 (H+); ~-o =--24 (CI-),--5 (H+); ~o = 6 (el-), 0 (H+). * Electrochemical Society Active Member. Key words: calomel electrode, electrolytes, entropy of transport, heat capacity of transport, ionic entropy, ionic heat capacity, ions, thermodynamic properties of salines, thermoelectric power, transported entropy, transported heat capacity.) unless CC License in place (see abstract). ecsdl.org/site/terms_use address. Redistribution subject to ECS terms of use (see 128.6.218.72 Downloaded on 2015-07-18 to IP ) unless CC License in place (see abstract). ecsdl.org/site/terms_use address. Redistribution subject to ECS terms of use (see 128.6.218.72 ABSTRACTThe moving (transported) ionic properties S and C are partial molal properties of the ion itself and include the effect of its electrical charge on that portion of the solvation layer which travels with the ion (Eastman first and second regions). The negatives of the ionic transport properties --S* and ) unless CC License in place (see abstract). ecsdl.org/site/terms_use address. Redistribution subject to ECS terms of use (see 128.6.218.72 Downloaded on 2015-07-18 to IP

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The Sulfatase of Ox Liver. IX. The Polymerization of Sulfatase A^*

Nichol¹,

Roy²

1965

Biochemistry

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the enzyme in 0.10 ionic strength buffers of pH 7.5 and 5.0 were subjected to two boundary analyses, those of Baldwin (1959) andof Fujita (1956), and by each method the material was demonstrated to be homogeneous with respect to sedimentation coefficient. However, the s values varied from 6 at pH 7.5 to 14 at pH 5.0, a result tentatively attributed to the polymerization of the enzyme at pH 5.0. The hypothesis has been tested

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The Polymerization of Bovine Pancreas Carboxypeptidase A

Cited by 3 publications

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The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride^*

The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride^*

The Thermal Temperature Coefficient of the Calomel Electrode Potential Between 0° and 70°C

The Sulfatase of Ox Liver. IX. The Polymerization of Sulfatase A^*

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The Polymerization of Bovine Pancreas Carboxypeptidase A

Cited by 3 publications

References 0 publications

The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride*

The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride*

The Thermal Temperature Coefficient of the Calomel Electrode Potential Between 0° and 70°C

The Sulfatase of Ox Liver. IX. The Polymerization of Sulfatase A*

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Product

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The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride^*

The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride^*

The Sulfatase of Ox Liver. IX. The Polymerization of Sulfatase A^*