Denaturation capability, absolute

The relative denaturation capability is, on the whole, a rather labile value, because it is difficult to standardize the first stage of the protein denaturation which takes place, without doubt, in the course of the electrophoresis on the paper, the drying of the paper, and the elution. In the following pages a more serviceable and incomparably more stable value will be described, namely, the absolute denaturation capability. 

We were thinking that it would be more correct to operate with the square root of the absolute denaturation capability (which is a product of two values), which would represent the best correction or compensation factor. In serial experiments the square root value did us good service, but its application did not bring any advantages over the simple product (the value representing the absolute denaturation capability) which would justify the introduction of this practically needless innovation that, moreover, might confuse some foreign workers. 

Relative % Variation coefficient in % of error Absolute denaturation capability Variation coefficient in % of error... 

Normal Values of Absolute Denaturation Capability for Non-pregnant Females... 

APPLICATIONS IN BIOLOGICAL AND CLINICAL CHEMISTRY 519 TABLE XI Correlation Between Results of Polarographic Examination and Absolute Denaturation Capability of Cerebrospinal Fluid Albumin ... 

Resulting value Mean absolute denaturation capability... 

In general we can say that polarographic examination of the cerebrospinal fluid is about equally important as the determination of the absolute denaturation capability of cerebrospinal fluid albumin, the correlation coefficient being r = -1-0.714 (98). 

Under certain conditions, the stress-70 proteins can participate in the renaturation of denatured or inactivated proteins. The renaturation capabilities of E. coli dnaK protein have been most extensively documented. It has been shown that in vitro, dnaK can protect E. coli RNA polymerase from aggregation when the polymerase is incubated at elevated temperatures that would normally result in loss of activity, and, further, that dnaK can disaggregate and reactivate polymerase, once it has been inactivated by heat denaturation (Skowyra et al., 1990). These activities are absolutely dependent on ATP hydrolysis. The mutant dnaK756 protein is effective in protecting active RNA polymerase against heat inactivation, but is incapable of disaggregating and reactivating polymerase, once it has been heat inactivated. 

---