Biological properties of myeloma proteins

1975 ◽  
Vol 135 (1) ◽  
pp. 32-36 ◽  
Author(s):  
C. K. Osterland
1961 ◽  
Vol 114 (4) ◽  
pp. 521-533 ◽  
Author(s):  
Edward C. Franklin ◽  
Denis R. Stanworth

The antigenic properties of normal 19S γ-globulin, pathologic macroglobulins, ß2A-myeloma proteins, and Bence Jones proteins have been compared with 7S γ-globulin and the small 3.5S units derived from it by gel diffusion precipitin techniques. These studies demonstrate that the determinant groups on the 7S γ-globulin molecule responsible for the cross-reaction with each of the other proteins are associated with the two fragments of 7S γ-globulin which have the antibody-combining sites. The antigenic specificity of the 7S γ-globulin which distinguishes it from each of these proteins is associated primarily with the fragment that is richest in hexose and can not combine with antigen. However when compared with certain of the paraproteins additional antigenic specificity was also found to reside in the fragments with antibody-combining activity. The finding of similar antigenic relationships in rabbit γ-globulins suggests that some of the biological properties associated only with the 7S γ-globulins and not with the other immune globulins may reside in the fragment which also carries the antigenic specificity of the protein.


1966 ◽  
Vol 166 (1003) ◽  
pp. 114-123 ◽  

The general configuration of immunoglobulins and the chemical relationships that exist between different classes of antibodies have become clear during recent years. On the other hand, the structural features which determine various biological activities of these complex molecules have not been elucidated and, in particular, the basis of combining specificity is not understood. The problem of relating biological activity to chemical structure is complicated by the size of antibody molecules (molecular weight 150 000 or more) and more particularly by the remarkable heterogeneity of their constituent peptide chains. As a result of this complexity, variations in the structure of immunoglobulins cannot be ascribed with certainty to particular biological properties and it has proved impossible to establish the detailed chemical structure of specific antibodies. These difficulties have stimulated renewed interest in the proteins found in multiple myelomatosis and certain related pathological conditions. Individual myeloma proteins have the same general configuration as antibody molecules, but their peptide chain structure is sufficiently homogeneous to permit of detailed chemical analysis. In this paper the general structure of different classes of antibody will be described and their peptide chain structure compared with that of myeloma proteins; several detailed reviews of this subject have been published recently (Cohen & Porter 1964; Franklin 1964; Nisonoff & Thorbecke 1964; Fleischman 1966).


Author(s):  
David A. Agard ◽  
Yasushi Hiraoka ◽  
John W. Sedat

In an effort to understand the complex relationship between structure and biological function within the nucleus, we have embarked on a program to examine the three-dimensional structure and organization of Drosophila melanogaster embryonic chromosomes. Our overall goal is to determine how DNA and proteins are organized into complex and highly dynamic structures (chromosomes) and how these chromosomes are arranged in three dimensional space within the cell nucleus. Futher, we hope to be able to correlate structual data with such fundamental biological properties as stage in the mitotic cell cycle, developmental state and transcription at specific gene loci.Towards this end, we have been developing methodologies for the three-dimensional analysis of non-crystalline biological specimens using optical and electron microscopy. We feel that the combination of these two complementary techniques allows an unprecedented look at the structural organization of cellular components ranging in size from 100A to 100 microns.


2015 ◽  
Vol 57 ◽  
pp. 177-187 ◽  
Author(s):  
Jennifer N. Byrum ◽  
William Rodgers

Since the inception of the fluid mosaic model, cell membranes have come to be recognized as heterogeneous structures composed of discrete protein and lipid domains of various dimensions and biological functions. The structural and biological properties of membrane domains are represented by CDM (cholesterol-dependent membrane) domains, frequently referred to as membrane ‘rafts’. Biological functions attributed to CDMs include signal transduction. In T-cells, CDMs function in the regulation of the Src family kinase Lck (p56lck) by sequestering Lck from its activator CD45. Despite evidence of discrete CDM domains with specific functions, the mechanism by which they form and are maintained within a fluid and dynamic lipid bilayer is not completely understood. In the present chapter, we discuss recent advances showing that the actomyosin cytoskeleton has an integral role in the formation of CDM domains. Using Lck as a model, we also discuss recent findings regarding cytoskeleton-dependent CDM domain functions in protein regulation.


Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
N Miceli ◽  
MF Taviano ◽  
A Trovato ◽  
R De Pasquale ◽  
P Maimone ◽  
...  

Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
D Moreira ◽  
F Candido ◽  
M Siqueira ◽  
C Quaresma ◽  
E Guimarâes ◽  
...  

Planta Medica ◽  
2014 ◽  
Vol 80 (16) ◽  
Author(s):  
CA Aguiar ◽  
AM Ferreira ◽  
R Oliveira ◽  
F Baltazar ◽  
A Cunha

Planta Medica ◽  
2015 ◽  
Vol 81 (16) ◽  
Author(s):  
S Combrinck ◽  
J Linde ◽  
A Ludwiczuk ◽  
S Van Vuuren ◽  
J Van Rooy ◽  
...  

2017 ◽  
Vol 4 (2) ◽  
pp. 87-91
Author(s):  
Ekamaida Ekamaida

The soil fertility aspect is characterized by the good biological properties of the soil. One important element of the soil biological properties is the bacterial population present in it. This research was conducted in the laboratory of Microbiology University of Malikussaleh in the May until June 2016. This study aims to determine the number of bacterial populations in soil organic and inorganic so that can be used as an indicator to know the level of soil fertility. Data analysis was done by T-Test that is by comparing the mean of observation parameter to each soil sample. The sampling method used is a composite method, which combines 9 of soil samples taken from 9 sample points on the same plot diagonally both on organic soil and inorganic soil. The results showed the highest bacterial population was found in total organic soil cfu 180500000 and total inorganic soil cfu 62.500.000


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