The viruses; biochemical, biological, and biophysical properties, edited by F. M. Burnet [and] W. M. Stanley.

Stanley, W. M.

doi:10.5962/bhl.title.10179

Cited by 121 publications

(153 citation statements)

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“…Vicari and Lennox (23) have also obtained exponential and similar rates of antibody formation during the primary and secondary antibody response to bacteriophage T2 in rabbits. In contrast to results with ~bX, however, the primary antibody response to soluble proteins has generally been considered to be non-exponential (24). One explanation for the differences in the early kinetics of antibody formation may be the extreme sensitivity of the assay for antibody to phage.…”

Section: Discussionmentioning

confidence: 46%

Antibody Formation

Uhr

Finkelstein

Baumann

1962

The Journal of Experimental Medicine

121

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Quantitative studies of antibody formation in experimental animals have been facilitated by the use of labeled proteins (1, 2). After equilibration following intravenous injection, labeled antigen is eliminated from the circulation in two exponential phases: the first and slower rate is due to non-immune catabolism; the second and rapid decline is caused by the production and release into the circulation of specific antibody (3, 4).In this study, guinea pigs have been injected with relatively minute amounts of a small bacteriophage, 4~X 174, which has been traced in the circulation utilizing the plaque-forming capacity of the virus. With this method it has been possible to detect an immune elimination as early as 24 hours after injection. The early detection of antibody was facilitated by the small amounts of antigen employed. It has also been shown that there is a close resemblance between the kinetics of the primary and secondary antibody response to this bacteriophage. Materials and MethodsPhage.--Str~J.us of ~bX 174 and T2 were kindly supplied to us by Dr. E. Lennox. ~bX was grown in Escherickia coli strain C in glycerol-easamino acid medium (5). The lysed culture was centrifuged at low speed to remove cell debris. Purification was then accomplished by precipitation with ammonium sulfate, passage through a DEAE cellulose anion exchange column, and elution with 0.1 M ammonium acetate (6). This purified stock containing 10 n plaque-forming particles per ml was kept at 4°C in ammonium acetate buffer pH 7.4 conraining 0.01 per cent gelatin. Dilutions of this stock were used for almost all the immunization experiments.

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Section: Discussionmentioning

confidence: 46%

Antibody Formation

Uhr

Finkelstein

Baumann

1962

The Journal of Experimental Medicine

121

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“…This effect could relate to tumor-induced immunosuppression that allows the cancer to advance [25] or could in some cases simply indicate a weak immune response due to other reasons. Since the levels of tumor-infiltrating lymphocytes can be prognostic for prostate cancer progression [26], it may also be valuable to look at the prognostic value of anti-tumor antibody levels, or the relationship between circulating antibody levels and tumor-infiltrating lymphocyte levels.…”

Section: Discussionmentioning

confidence: 99%

An experimental strategy for quantitative analysis of the humoral immune response to prostate cancer antigens using natural protein microarrays

Forrester

Qiu

Mangold

et al. 2007

Proteomics Clinical Apps

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The identification of human tumor antigens has potential utility in the diagnosis and treatment of cancers. We demonstrate here a complete strategy to profile immunoreactivity and identify tumor antigens from proteins derived from tumor cell lines. Microarrays of proteins produced from 2-D LC fractionation of prostate tumor cell-line lysates were used to profile immunoreactivity in the sera of prostate cancer patients and control subjects. Cancer-associated immunoreactivity to distinct groups of chromatography fractions was present in about 50% of the patients, with greater immunoreactivity present in patients with non-organ-confined cancer than in patients with organ-confined cancer. We grouped the immunoreactive fractions by similarities in elution order and patterns of immunoreactivity to guide and interpret the MS analysis of selected fractions, which was used to identify the proteins that may be responsible for the immunoreactivity. As a complementary method to further characterize and validate the immunoreactivity of the proteins identified by mass spectrometry, we demonstrate the use of focused microarrays of recombinant proteins. Disease-associated immunoreactivity was confirmed for one of the identified proteins, human Kallikrein 11. These results demonstrate a practical approach to screening, identifying, and validating immunoreactive proteins that could be applied to diverse studies on humoral immune responses.

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“…It is unclear, however, whether this cell is related to normal mast cells or represents a distinct cell line (15).…”

Section: Resultsmentioning

confidence: 99%

A major serine protease in rat skeletal muscle: Evidence for its mast cell origin

Woodbury

Everitt

Sanada

et al. 1978

Proc. Natl. Acad. Sci. U.S.A.

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The physical, chemical, and immunologic properties of a protease from rat skeletal muscle, proposed to function in the degradation of certain intracellular enzymes, are identical to those of a chymotrypsin-like serine protease isolated from peritoneal mast cells. The results of polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and 8 M urea indicate that the two rat proteases have identical mobilities corresponding to a molecular weight of 26,000. The relative amino acid compositions of the proteases are nearly identical. Immunodiffusion tests for crossreaction between the muscle protease and antisera directed toward mast cell protease indicate that the former is immunologically identical to mast cell protease. The first 35 amino-terminal residues of the two enzymes are identical and indicate homology of these proteins to other mammalian serine proteases. The sequence analysis of the protease from muscle was extended -for an additional 16 positions, and comparison of this amino-terminal sequence with that of a similar enzyme from small intestine showed approximately 75% sequence identity. In contrast, only 40% of the residues in this region of bovine chyrnotrypsin A were found at corresponding loci in rat muscle protease. It is concluded that the protease from muscle or mast cells is closely related to the enzyme from small intestine which recently was localized in the "atypical" mast cells of gut mucosa Katunuma and coworkers (1, 2) have isolated several chymotrypsin-like serine proteases from various rat tissues and proposed that these enzymes initiate the degradation of several intracellular pyridoxal phosphate-dependent enzymes such as ornithine aminotransferase. The apo forms of these enzymes were inactivated by the proteases, but not the holo enzymes nor the apo forms of enzymes requiring other cofactors.Recently, an improved method was developed to purify a serine protease from rat skeletal muscle (unpublished data). During that study it was observed that the relative amino acid composition of this enzyme and that of the chymotrypsin-like protease (chymase) of peritoneal mast cells (3) were similar. The present study shows that the amino-terminal sequences and the immunologic properties of these two proteases are identical. EXPERIMENTAL Materials. For the purpose of developing specific antisera, a small amount of the chymotrypsin-like protease of rat peritoneal mast cells was purified as described by Lagunoff and Pritzl (4). Larger quantities of enzymes were prepared by a method which includes affinity adsorption chromatography on ovoinhibitor immobilized on Sepharose 4B (unpublished data). The protease from skeletal muscle was purified by the method of Sanada et al. (5) or by the affinity adsorption method described above. Rabbit antisera directed toward mast cell protease or the "atypical" mast cell protease of small intestine were prepared and their specificities were determined as described (3).Methods. Proteins were reduced and pyridylethylated (6) before sequence a...

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The viruses; biochemical, biological, and biophysical properties, edited by F. M. Burnet [and] W. M. Stanley.

Cited by 121 publications

References 0 publications

Antibody Formation

Antibody Formation

An experimental strategy for quantitative analysis of the humoral immune response to prostate cancer antigens using natural protein microarrays

A major serine protease in rat skeletal muscle: Evidence for its mast cell origin

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