The Isolation of Two Human IgG Myeloma Proteins with Skin Fixing Properties on Monkey Lung Tissue Like Human Reagin

1973 ◽  
Vol 45 (1-2) ◽  
pp. 26-29 ◽  
Author(s):  
A. Malley ◽  
L. Baecher ◽  
G. Crossley
1994 ◽  
Vol 73 (2) ◽  
pp. 215-223 ◽  
Author(s):  
Ralph C. Williams ◽  
Andrew D. Schriber ◽  
Christine C. Malone ◽  
Franco Silvestris ◽  
Noreen Hannigan ◽  
...  
Keyword(s):  

Nature ◽  
1969 ◽  
Vol 223 (5208) ◽  
pp. 837-838 ◽  
Author(s):  
G. ROSSI ◽  
T. K. CHOI ◽  
A. NISONOFF
Keyword(s):  

1965 ◽  
Vol 122 (6) ◽  
pp. 1087-1102 ◽  
Author(s):  
William D. Terry ◽  
John L. Fahey ◽  
Arthur G. Steinberg

Human G myeloma (7S γ2-myeloma) proteins were investigated for relationships between Gm and Inv genetic factors and the different antigenic types of heavy polypeptide chains (γ-chains) and light polypeptide chains. Myeloma proteins were isolated from the sera of 1 Chinese, 60 white and 28 Negro individuals. These 89 proteins were tested for eight Gm factors [Gm(a), Gm(x), Gm(b2), Gm(f), Gm(b1), Gm(b3), Gm(b4), and Gm(c)], and two Inv factors [Inv(l) and Inv(b)]. Results of the tests were correlated with the four γ-chain subclasses (γ2a, γ2b, γ2c and γ2d) and the two types of light polypeptide chains, κ-chains (type K or I) and λ-chains (type L or II) found in human IgG molecules. 1. Gm factors were limited to myeloma proteins with heavy polypeptide chains of the γ2b- and γ2c-subclasses. No Gm factors were detected on γ2a- and γ2d-myeloma proteins or on a "heavy-chain" disease protein of subclass γ2d. 2. γ2b-Proteins were positive for at least one Gm factor and were either Gm(a+), Gm(a + x+), or Gm(b2+ f+). 3. γ2c-Myeloma proteins, and one γ2c-"heavy-chain" disease protein, were positive for at least one Gm factor and contained various combinations of factors Gm(b1), (b2), (b4), and (c). Myeloma proteins from 3 Negroes were included in this group. 4. Inv factors (l) and (b) were limited to myeloma proteins with κ-light polypeptide chains. These Inv factors were not detected on proteins with λ-light polypeptide chains. 5. Most (70 per cent) of the γ2b- and γ2c-proteins with κ-chains were Inv(l+) or Inv(b+). None of the γ2a- or γ2d-proteins with κ-chains, however, contained these Inv factors.


Author(s):  
M. G. Williams ◽  
C. Corn ◽  
R. F. Dodson ◽  
G. A. Hurst

During this century, interest in the particulate content of the organs and body fluids of those individuals affected by pneumoconiosis, cancer, or other diseases of unknown etiology developed and concern was further prompted with the increasing realization that various foreign particles were associated with or caused disease. Concurrently particularly in the past two decades, a number of methods were devised for isolating particulates from tissue. These methods were recently reviewed by Vallyathan et al. who concluded sodium hypochlorite digestion was both simple and superior to other digestion procedures.


Author(s):  
Jerrold L. Abraham

Inorganic particulate material of diverse types is present in the ambient and occupational environment, and exposure to such materials is a well recognized cause of some lung disease. To investigate the interaction of inhaled inorganic particulates with the lung it is necessary to obtain quantitative information on the particulate burden of lung tissue in a wide variety of situations. The vast majority of diagnostic and experimental tissue samples (biopsies and autopsies) are fixed with formaldehyde solutions, dehydrated with organic solvents and embedded in paraffin wax. Over the past 16 years, I have attempted to obtain maximal analytical use of such tissue with minimal preparative steps. Unique diagnostic and research data result from both qualitative and quantitative analyses of sections. Most of the data has been related to inhaled inorganic particulates in lungs, but the basic methods are applicable to any tissues. The preparations are primarily designed for SEM use, but they are stable for storage and transport to other laboratories and several other instruments (e.g., for SIMS techniques).


Author(s):  
Daniel C. Pease

It is reasonable to think that phospholipid micelles should be visible and identifiable in electron micrographs of ultrathin sections if only they can be preserved throughout the embedding process. The development of highly polar, water-containing, aminoplastic embedments has made this a likely possibility. With this in mind, an investigation of the lecithin-secreting, Type II pneumocytes of the lung is underway.Initially it has been easiest to recognize phospholipid micelles in lung tissue fixed first with glutaraldehyde, and then secondarily exposed to osmium tetroxide. However, the latter is not a necessary concomitant for micellar preservation. Conventional uranyl acetate and lead citrate staining is finally applied. Importantly, though, the micelles have been most easily seen in tissue embedded in 507. glutaraldehyde polymerized with urea, as described in detail by D.C. Pease and R.G. Peterson (J. Ultra- struct. Res., 41, 133, 1972). When oriented appropriately, the micellar units are seen as tiny, bilayer plates.


Author(s):  
J. D. Shelburne ◽  
Peter Ingram ◽  
Victor L. Roggli ◽  
Ann LeFurgey

At present most medical microprobe analysis is conducted on insoluble particulates such as asbestos fibers in lung tissue. Cryotechniques are not necessary for this type of specimen. Insoluble particulates can be processed conventionally. Nevertheless, it is important to emphasize that conventional processing is unacceptable for specimens in which electrolyte distributions in tissues are sought. It is necessary to flash-freeze in order to preserve the integrity of electrolyte distributions at the subcellular and cellular level. Ideally, biopsies should be flash-frozen in the operating room rather than being frozen several minutes later in a histology laboratory. Electrolytes will move during such a long delay. While flammable cryogens such as propane obviously cannot be used in an operating room, liquid nitrogen-cooled slam-freezing devices or guns may be permitted, and are the best way to achieve an artifact-free, accurate tissue sample which truly reflects the in vivo state. Unfortunately, the importance of cryofixation is often not understood. Investigators bring tissue samples fixed in glutaraldehyde to a microprobe laboratory with a request for microprobe analysis for electrolytes.


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