The Investigation of Proteins by Diffusion Measurements.

Neurath, Hans

doi:10.1021/cr60097a004

Cited by 94 publications

(29 citation statements)

References 27 publications

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“…Calculations with equations 10, 12 (25), and 1 (26) yielded a mean value of 2.62 × 10 -v with a standard deviation of 4-0.032, whereas with equation 13 (25) the calculated mean diffusion constant was considerably higher; i.e., 4.5 × !0-L In the presence of 6 ~ guanidine hydrochloride, the diffusion pattern was indicative of monodispersity, all four methods of calculation yielding consistent values. Converted to normal coordinates, the experimental diffusion curves were superimposable on a Gaussian distribution curve.…”

Section: Resultsmentioning

confidence: 95%

“…1 and Table II, the relative viscosity resembles closely that of the native protein. Diffusion measurements indicated the material to be aggregated to a considerable extent, the mean value calculated with equations 10, 12 (25), and 1 (26) being 0.94 X 10 -7. This lack of monodispersity precluded estimations of molecular weights.…”

Section: Resultsmentioning

confidence: 99%

“…cm./sec, to 2.3 × 10 -7. This shift is prob-ably due to a diminution of the extent of mutual interaction between the large and asymmetric antibody molecules (25).…”

Section: Resultsmentioning

confidence: 99%

“…While it is true that the diffusion method is too insensitive to detect the presence of traces of partially denatured or undenatured protein in an otherwise monodisperse solution of fully denatured material, it is doubtful that the "regenerated" material may be generally identified with undenatured protein. As discussed in detail elsewhere (14,25), the percentage of regenerated normal globulin, serum albumin, or hemoglobin is too large to escape detection by diffusion or ultracentrifugation, if the regenerated protein departs significantly from the size or shape characteristics of the fully denatured form. It is also clear that the serological properties of the regenerated antibody fraction differ significantly from those of the native protein.…”

Section: Discussionmentioning

confidence: 99%

“…Diffus/on.--The refractometric scale method, described in detail elsewhere (25), was used for the determination of diffusion constants and for an estimation of the degree of monodispersity. Calculations were made with equations 10, 11, 12, and 14 of reference 25, and equation 1 of reference 26.…”

Section: Methodsmentioning

confidence: 99%

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Immunochemical Properties of Native and Denatured Horse Serum Globulins

Erickson

Neurath

1945

Journal of General Physiology

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The problem of the relation of antibodies to normal serum globulins has been approached in the past by comparison of their chemical, physical, and immunological properties in the native state (cf. 1-3). Little information is available, however, on their relative behavior in the denatured state. This paper describes an investigation of the effects of denaturation by guanidine hydrochloride on certain physicochemical and immunological properties of Type I antipneumococcal horse serum globulin. In the fight of recent theories of the structure and synthesis of antibodies (4, 5) it appeared also of interest to determine whether denaturation of normal and immune globulin might accentuate or diminish the antigenic relations which exist between them in the native form.Comparative physicochemical properties of normal and immune serum globulins have been reviewed by Kabat (3). Wright (6) has reported that the antigenic nature of horse antibody proteins is essentially the same as that of horse normal gamma globulin. However, quantitative investigations by Treffers et al. (7)(8)(9) based on earlier findings of Ando et al. (10), and Marrack and Duff (11), revealed that antipneumococeal horse serum globulin differs from normal gamma globulin in its reaction with an antispecific precipitate rabbit serum. A high degree of cross-reactivity existed, and it was further noted that those antibodies that were precipitated by either antigen were incapable of differentiating between the two. These investigations provided experimental proof for earlier suggestions (12) that the groups on the antibody molecule responsible for antibody activity are unrelated to those involved in antigenic specificity.Previous work on the effects of denaturation on the serological and physicochemical behavior of immune globulins has been extensively reviewed (1,13,14). The observation that monolayers of Types i and III antipneumococcal rabbit globulin are serologic.ally active (15), suggests the independence of serological activity of a unique stereochemical configuration. However, in the light of a recent hypothesis (16) that formation of protein films involves the separation of preformed layers of peptide chains rather than unfolding into individual chains, a functional relation between intact two dimensional configurations and antibody activity is not excluded.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

“…cm./sec, to 2.3 × 10 -7. This shift is prob-ably due to a diminution of the extent of mutual interaction between the large and asymmetric antibody molecules (25).…”

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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