Polymerization-Depolymerization of Tobacco Mosaic Virus Protein. VIII. Light-Scattering Studies<sup>*</sup>

Smith, Carl E.; Lauffer, Max A.

doi:10.1021/bi00860a023

Cited by 61 publications

(39 citation statements)

References 28 publications

(39 reference statements)

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“…Figure 6 shows "final" activity recovered after a temperature leap from a range of initial 120-min incubations. This pattern is strongly reminiscent of that shown by the reversible temperature dependence of TMV protein aggregation to form rodlike polymers (Smith & Lauffer, 1967). In this well-studied system, a strong hydrophobic component of the association energetics has been inferred (Lauffer, 1975).…”

Section: Y Xie and Db Wetlaufermentioning

confidence: 59%

“…The two curves make a qualitatively similar pattern to that of the same temperatures in Figure 1. However, the depression of the 36" curve below the 20" curve was somewhat unexpected, although it may be argued that this is qualitatively what one would expect from a hydrophobic mechanism dominating the oligomer and aggregate-forming reactions (Kauzmann, 1959;Smith & Lauffer, 1967;Tanford, 1980).…”

Section: Y Xie and Db Wetlaufermentioning

confidence: 91%

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Control of aggregation in protein refolding: The temperature‐leap tactic

Xie

Wetlaufer

1996

Protein Science

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The kinetics of renaturation of bovine carbonic anhydrase II (CAII) were studied from 4 degrees to 36 degrees, at the relatively high [CAII] of 4 mg/mL. Following dilution to 1 M guanidinium chloride, aggregate formation is very rapid and reduces the formation of active enzyme. The CAII activity yield at 150 min, 20 degrees (approximately 60%), is greater than that at either 4 degrees or 36 degrees. However, if refolding is conducted at 4 degrees, aggregation is reduced dramatically and 37% yield is obtained at 120 min. If the solution is then rapidly warmed to 36 degrees, the yield rises rapidly to 95% at 150 min. This is an example of the "temperature leap" tactic. These results can be understood on the basis of two slow-folding intermediate whose kinetics have been studied. Only the first of these forms aggregates. Kinetic simulations show that, at 4 degrees, the first intermediate is depleted after 120 min, and the second intermediate rapidly isomerizes to active enzyme on warming. A series of experiments was conducted where the initial (120 min) folding temperature was systematically varied, followed by a "leap" to 36 degrees for 30 additional minutes. With initial incubations from 4 degrees to 12 degrees, the final yield is > 90%, drops rapidly from 12 degrees to 20 degrees, and decreases more gradually to approximately 45% at 36 degrees. The overall results qualitatively fit the simple idea of ordinary temperature-accelerated reactions in competition with hydrophobic aggregation, which is strongly suppressed in the cold. Qualifications are discussed for the temperature-leap approach to find application in refolding other proteins.

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Section: Y Xie and Db Wetlaufermentioning

confidence: 59%

Section: Y Xie and Db Wetlaufermentioning

confidence: 91%

Control of aggregation in protein refolding: The temperature‐leap tactic

Xie

Wetlaufer

1996

Protein Science

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“…The absorbance of CP at 320 nm is directly proportional to the degree of polymerization with itself, and the degree of change of TMV-CP in vitro polymerization is also in positive proportion to the temperature according to the report [22]. As shown in Fig.…”

Section: Effect Of Nnm On Tmv-cp In Vitro Polymerizationmentioning

confidence: 89%

Induction of systemic resistance against tobacco mosaic virus by Ningnanmycin in tobacco

Han

Luo

Shirong

et al. 2014

Pesticide Biochemistry and Physiology

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“…4 and 5, a treatment parallel to that used by Smith and Lauffer (1967) for linear condensation polymerization of TMV A-protein can be applied to the mitotic spindle, although use of this treatment is not meant to necessarily imply such a mechanism . Reiterating Smith and Lauffer (1967), if p is taken as the degree of polymerization (here assumed to be b /Ao), the concentration of monomer (in this case dimeric tubulin) in polymeric form will be mp (here b), where m is the total molar concentration of monomer (in this case a direct function of A 0 but not evaluated in molar concentration) . The concentration of free monomer at equilibrium z follows as m(1 -p) .…”

Section: Alternative Equilibrium Treatmentsmentioning

confidence: 99%

“…The thermodynamic equilibrium constant K may be taken as the ratio of the forward and reverse rate constants for polymerization and dissociation, respectively. For TMV A-protein polymerization, Smith and Lauffer (1967) considered the association to be second order, and the dissociation first order, giving dz/dt = 0 at equilibrium, or k 1m 2(l -p) 2 = k2mp, where k 1 and k2 are the association and dissociation rate constants, respectively . The equilibrium constant K follows as k 1 /k 2 and is equal to p/m(1 -p) 2, a function directly applicable to the birefringence data and yielding the relationship K = b/(A o -b) 2 .…”

Section: Alternative Equilibrium Treatmentsmentioning

confidence: 99%

A Thermodynamic Analysis of Mitotic Spindle Equilibrium at Active Metaphase

Stephens

1973

The Journal of Cell Biology

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The mitotic apparatus of first-division metaphase eggs of the sea urchin Strongylocentrotus drobachiensis was observed by means of polarization microscopy under controlled temperature conditions . Eggs were fertilized and grown at two temperature extremes in order to produce two different sizes of available spindle pool . Slow division time allowed successive samples of such cells to be observed at the same point in metaphase but at different equilibrium temperatures, yielding curves of metaphase equilibrium birefringence vs . observational temperature . Using the plateau value of birefringence at higher temperatures as a measure of total available spindle pool and the observed birefringence at lower temperatures as a measure of polymerized material at equilibrium, the spindle protein association was evaluated according to the method of Inoue . Both pool conditions produced linear van't Hoff functions . Analysis of these functions yielded enthalpy and entropy changes of +55-65 kcal/mol and + 197-233 entropy units (cu), respectively . These values for active mitotic metaphase are quite comparable to those obtained by Inoue and co-workers for arrested meiotic metaphase cells . When other equilibrium treatments were considered, the best fit to the experimental data was still that of Inoue, a treatment which theoretically involves first-order polymerization and dissociation kinetics . Treatment of metaphase cells with D20 by direct immersion drove the equilibrium to completion regardless of temperature, attaining or exceeding a birefringence value equal to the cell's characteristic pool size ; perfusion with D20 appeared to erase the original temperature-determined pool size differences for the two growth conditions, attaining a maximum value characteristic of the larger pool condition . These data confirm Inoue's earlier contention that D 20 treatment can modify the available spindle pool .

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Polymerization-Depolymerization of Tobacco Mosaic Virus Protein. VIII. Light-Scattering Studies^*

Cited by 61 publications

References 28 publications

Control of aggregation in protein refolding: The temperature‐leap tactic

Control of aggregation in protein refolding: The temperature‐leap tactic

Induction of systemic resistance against tobacco mosaic virus by Ningnanmycin in tobacco

A Thermodynamic Analysis of Mitotic Spindle Equilibrium at Active Metaphase

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Polymerization-Depolymerization of Tobacco Mosaic Virus Protein. VIII. Light-Scattering Studies*

Cited by 61 publications

References 28 publications

Control of aggregation in protein refolding: The temperature‐leap tactic

Control of aggregation in protein refolding: The temperature‐leap tactic

Induction of systemic resistance against tobacco mosaic virus by Ningnanmycin in tobacco

A Thermodynamic Analysis of Mitotic Spindle Equilibrium at Active Metaphase

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Polymerization-Depolymerization of Tobacco Mosaic Virus Protein. VIII. Light-Scattering Studies^*