The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride<sup>*</sup>

Bethune, J. L.

doi:10.1021/bi00888a019

Cited by 22 publications

(10 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Thus, it appears most likely that association occurs primarily as a result of hydrophobic interactions. Similar observations have been made with numerous other proteins, e.g., tobacco mosaic virus protein (Stevens and Lauffer, 1965), carboxypeptidase A (Bethune, 1965), phycocyanin (Scott and Berns, 1965), and ox liver sulfatase A (Nichol and Roy, 1965).…”

Section: Resultssupporting

confidence: 81%

Effect of high-pressure pulsation on some of the physical-chemical properties of ovalbumin

Swaisgood¹,

Barone²,

Aurand³

et al. 1972

J. Agric. Food Chem.

View full text Add to dashboard Cite

Section: Resultssupporting

confidence: 81%

Effect of high-pressure pulsation on some of the physical-chemical properties of ovalbumin

Swaisgood¹,

Barone²,

Aurand³

et al. 1972

J. Agric. Food Chem.

View full text Add to dashboard Cite

“…In contrast, the concentration dependence of the native enzyme is positive over this concentration range (Rupley and Neurath, 1960;Bethune, 1965).…”

Section: Results3mentioning

confidence: 89%

“…As with the native enzyme, sedimentation of A-succinylcarboxypeptidase reveals only a single boundary (Bethune, 1965). However, at protein concentrations up to 20 mg/ml, the sedimentation coefficient of the native enzyme exhibits a positive dependence on concentration, indicating the presence of a polymer (Rupley and Neurath, 1960;Bethune, 1965). In contrast, the concentration dependence of the sedimentation coefficient of A-succinylcarboxypeptidase is negative.…”

Section: Discussionmentioning

confidence: 94%

See 1 more Smart Citation

Physicochemical Studies of Carboxypeptidase A Derivatives. II. N-Succinylcarboxypeptidase^*

Bethune¹,

Ulmer²,

Vallée³

1967

Biochemistry

Self Cite

View full text Add to dashboard Cite

Previous studies have shown that modification of active center tyrosyl residues of carboxypeptidase A with acetylimidazole markedly alters catalytic activity without discernible change in protein structure. kcetylation of both tyrosyl and lysyl residues with acetic anhydride induces similar catalytic changes but concomitantly alters protein structure (Bethune, J. L., Ulmer, D. D., and Vallee, B. L., Biochemistry 3, 1764 (1964)). The consequences of modifying amino groups only now have been assessed in an N-succinyl derivative of the enzyme. The structural stability of N-succinylcarboxypeptidase enzyme as a function of p H does not B ovine pancreatic carboxypeptidase A has proven a useful system for assessing relationships of protein structure and composition to enzymatic function. The enzyme exhibits remarkable alterations in catalytic rates, specificity, or both when subjected to a wide range of inorganic substitutions (Coleman and Vallee, 1960), and organic modifications such as acetylation (Simpson et ut., 1963;Riordan and Vallee, 1963), acylation with dicarboxylic acid anhydrides (Riordan and Vallee, 1964), iodination (Simpson and Vallee, 1966), coupling with 5-diazo-1 H-tetrazole Vallee, 1966, 1967), nitration with tetranitromethane (Riordan et uf., 1966), or irradiation with ultraviolet light (Piras and Vallee, 1966). In many instances, altered function has appeared to derive solely from modification of specific side chains of the active center' or substitution of specific metal ions at the active site of the enzyme. However, some reactions have been found to induce changes in protein secondary or tertiary structure and,

show abstract

“…covalent aggregation was not prevented. The temperature only remains as a variable: hydrophobic bonds are less stable at low temperatures (Nemethy & Scheraga, 1962;Bethune, 1965), so that the possibility of their breakage and reformation should be enhanced by lowering the temperature. Accordingly a renaturation experiment was conducted in the same manner as before, but the temperature was lowered in parallel with the sodium dodecyl sulphate concentration (for reasons of solubility) from 210 to 4°C.…”

Section: Attempted Renaturation From Sodium Dodecyl Sulphatementioning

confidence: 99%

Studies of the denaturation and partial renaturation of ovalbumin

Holt

Creeth

1972

Biochemical Journal

View full text Add to dashboard Cite

1. The denaturation of ovalbumin by the reagents sodium dodecyl sulphate and guanidinium chloride was investigated, by following the changes in sedimentation velocity, optical rotatory dispersion and viscosity as a function of denaturant concentration. 2. With sodium dodecyl sulphate both the optical-rotatory-dispersion parameters ao and bo become more negative, the sedimentation coefficient decreases and the viscosity increases; significant differences in the denaturation profiles are observed. The change in each parameter is indicative of only limited denaturation. 3. With guanidinium chloride the transition occurs over the concentration range 1-4m: more extensive changes occur in all the physical parameters than with sodium dodecyl sulphate. The values of ao and bo are indicative of complete denaturation. Reduction by mercaptoethanol produces only minor further changes. 4. Renaturation was attempted from both denaturants, the removal of reagent being accomplished reversibly by controlled slow dialysis. Partial renaturation was observed, but aggregated or insoluble material was produced in both cases at relatively low concentrations of denaturant. Similar behaviour was observed with fully reduced protein in guanidinium chloride-mercaptoethanol; complete renaturation could not be brought about even at very low protein concentrations.

show abstract

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

Cited by 22 publications

References 27 publications

Effect of high-pressure pulsation on some of the physical-chemical properties of ovalbumin

Effect of high-pressure pulsation on some of the physical-chemical properties of ovalbumin

Physicochemical Studies of Carboxypeptidase A Derivatives. II. N-Succinylcarboxypeptidase^*

Studies of the denaturation and partial renaturation of ovalbumin

Contact Info

Product

Resources

About

The Polymerization of Carboxypeptidase A in Solutions Containing Sodium Chloride*

Cited by 22 publications

References 27 publications

Effect of high-pressure pulsation on some of the physical-chemical properties of ovalbumin

Effect of high-pressure pulsation on some of the physical-chemical properties of ovalbumin

Physicochemical Studies of Carboxypeptidase A Derivatives. II. N-Succinylcarboxypeptidase*

Studies of the denaturation and partial renaturation of ovalbumin

Contact Info

Product

Resources

About

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

Physicochemical Studies of Carboxypeptidase A Derivatives. II. N-Succinylcarboxypeptidase^*