Human antibodies and hybridomas最新文献

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Characterization of anti-tumor immunity derived from the inoculation of myeloma cells secreting the fusion protein RM4/IFN-tau. 接种分泌融合蛋白RM4/IFN-tau的骨髓瘤细胞的抗肿瘤免疫特性
Human antibodies and hybridomas Pub Date : 1996-01-01
Y Qi, T Moyana, Y Chen, J Xiang
{"title":"Characterization of anti-tumor immunity derived from the inoculation of myeloma cells secreting the fusion protein RM4/IFN-tau.","authors":"Y Qi,&nbsp;T Moyana,&nbsp;Y Chen,&nbsp;J Xiang","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Our previous study showed that the injection of mouse myeloma VKCK/RM4-IFN-tau cells secreting the fusion protein RM4/IFN-tau to syngeneic BALB/c mice resulted in tumor regression in 70% of mice after tumor inoculation. In this study, the VKCK/RM4-IFN-tau cell line was used to characterize the protective immunity subsequent to tumor inoculation. Our histologic findings demonstrated that, in the primary response to VKCK/RM4-IFN-tau inoculation, tumor regression is associated with macrophage infiltration. This macrophage-dominated regression further leads to a protective immunity against the 2nd challenge of parental VKCK tumor cells. FACS analysis and chromium release assays showed that the majority of T lymphocytes that mediated this anti-tumor immunity were CD8+ cytotoxic T lymphocytes (CTLs). Our animal studies further showed that the VKCK/RM4-IFN-tau cells were able to grow as aggressively as the parental VKCK cells in T lymphocyte deficient nude mice. The protective immunity started 7 days, became complete 10 days following and lasted up to at least 12 months subsequent to the tumor inoculation. The adoptive transfer of T lymphocyte-enriched spleen cells or CTLs also conferred significant protection against tumor growth of parental VKCK cells (p < 0.01). These data thus support the notion that genetically engineered tumor cells secreting IFN-tau may have potential use as tumor vaccines in preventing the development of tumor recurrence and/or metastases following the surgical removal of the primary tumors.</p>","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 1","pages":"21-6"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19851346","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
A humanized antibody with specificity for hepatitis B surface antigen. 具有乙型肝炎表面抗原特异性的人源抗体。
Human antibodies and hybridomas Pub Date : 1996-01-01
C J Ryu, E A Padlan, B R Jin, O J Yoo, H J Hong
{"title":"A humanized antibody with specificity for hepatitis B surface antigen.","authors":"C J Ryu,&nbsp;E A Padlan,&nbsp;B R Jin,&nbsp;O J Yoo,&nbsp;H J Hong","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>A murine monoclonal antibody H67 was characterized for the binding specificity, which showed that H67 recognizes a disulfide-bond-dependent conformational epitope of common a antigenic determinant on the hepatitis B surface antigen. The result suggested that this antibody may have the potential of replacing hepatitis B immune globulin in the prevention of hepatitis B virus (HBV) infection. Therefore, we have constructed the humanized antibody HuS10 by grafting the complementarity determining regions and some framework amino acid residues of H67 onto the most homologous human antibody variable regions, 21/28 for heavy chain variable region and B1 and J kappa 2 for light chain variable region, followed by combining with human constant regions C gamma 1 and C kappa. The affinity of the HuS10 was the same as that of the H67, 8 x 10(8) x 10(8)M-1, and the HuS10 neutralized the in vitro infection of adult human hepatocyte primary culture by adr or ayw subtype of HBV. The neutralization assay showed that the HuS10 had approximately 2,000-times higher specific activity than commercially available polyclonal HBIG. These results suggest that the humanized antibody will be useful in the prevention or treatment of HBV infection.</p>","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 3","pages":"113-22"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20013645","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
5th International Conference on Human Antibodies and Hybridomas. Jerusalem, Israel, 14-16 October 1996. Abstracts. 第五届人类抗体和杂交瘤国际会议。1996年10月14日至16日,以色列耶路撒冷。摘要。
Human antibodies and hybridomas Pub Date : 1996-01-01
{"title":"5th International Conference on Human Antibodies and Hybridomas. Jerusalem, Israel, 14-16 October 1996. Abstracts.","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 2","pages":"50-88"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"19944617","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Efficient in vitro affinity maturation of phage antibodies using BIAcore guided selections. 利用BIAcore引导选择高效的噬菌体抗体体外亲和成熟。
Human antibodies and hybridomas Pub Date : 1996-01-01
R Schier, J D Marks
{"title":"Efficient in vitro affinity maturation of phage antibodies using BIAcore guided selections.","authors":"R Schier,&nbsp;J D Marks","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Selection of higher affinity mutant phage antibodies has proven less than straightforward due to sequence dependent differences in phage antibody expression, toxicity to Escherichia coli, and difficulty in eluting the highest affinity phage. These differences lead to selection for increased levels of expression or decreased toxicity rather than for higher affinity. In this work, we demonstrate how surface plasmon resonance as employed in the BIAcore can be used to increase the efficiency of phage antibody selections, yielding greater increments in affinity from a single library. A mutant phage antibody library was created by randomizing nine amino acids located in the V(L) CDR3 of C6.5, a human scFv which binds the tumor antigen c-erbB-2 with a Kd of 1.6 x 10-8 M. The library was subjected to five rounds of selection in solution using decreasing concentrations of biotinylated c-erbB-2. After each round of selection, polyclonal phage were prepared and the rate of binding to c-erbB-2 determined in a BIAcore under mass transport limited conditions. Determination of the rate of binding permitted calculation of the concentration, and hence percent, of binding phage present. Results were used to select the antigen concentration for the next round of selection. To determine the optimal eluent, polyclonal phage was injected in a BIAcore and eluted using one of five different solutions (10 mM HCl, 50 mM HCl, 100 mM HCl, 100 mM triethylamine, 2.6 M MgCl2). Differences were observed in eluent efficacy, which was reflected in significant differences in the affinities of phage antibodies isolated from the library after a round of selection using the different eluents. Use of the BIAcore to determine the optimal eluent and guide the antigen concentration used for selection yielded a C6.5 mutant with a 16 fold reduction in Kd (Kd = 1.0 x 10-9 M). This represents at least a twofold greater increment in affinity than previously obtained from a single library of phage antibodies which bind antigens.</p>","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 3","pages":"97-105"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20013638","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Short synthetic CDR-peptides forming the antibody combining site of the monoclonal antibody against RNA bacteriophage fr neutralize the phage activity. 合成短的cdr肽,形成抗RNA噬菌体单克隆抗体的抗体结合位点,以中和噬菌体活性。
Human antibodies and hybridomas Pub Date : 1996-01-01
J Steinbergs, K Kilchewska, U Lazdina, A Dishlers, V Ose, M Sällberg, A Tsimanis
{"title":"Short synthetic CDR-peptides forming the antibody combining site of the monoclonal antibody against RNA bacteriophage fr neutralize the phage activity.","authors":"J Steinbergs,&nbsp;K Kilchewska,&nbsp;U Lazdina,&nbsp;A Dishlers,&nbsp;V Ose,&nbsp;M Sällberg,&nbsp;A Tsimanis","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The construction of a mouse hybridoma FR52 secreting neutralizing monoclonal antibody specific for RNA bacteriophages fr, MS2 and GA is reported. The genes encoding the variable domains of the monoclonal antibody FR52 heavy and light chains were cloned and sequenced and the corresponding complementarity determining region (CDR) peptides were chemically synthesized. The CDR-peptides were tested for their ability to neutralize the activity of RNA phage fr and related RNA phages MS2 and GA. The CDR-derived peptides H2, L2 and L3 interacted with the fr phage particles and neutralized fr phage activity. Two of these peptides--H2 and L3 also had the ability to neutralize partly the activity of related bacteriophage MS2, but L1 and especially L3 neutralize the activity of the RNA phage GA. These results provide an excellent system for further antibody-antigen interaction studies and raise the possibility that simple CDR-peptides may serve as a new class of anti-viral molecules.</p>","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 3","pages":"106-12"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20013642","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Comparative study of the role of serum levels of p53 antigen and its tumor cell concentration in colon cancer detection. 血清p53抗原水平及其肿瘤细胞浓度在结肠癌检测中的比较研究。
Human antibodies and hybridomas Pub Date : 1996-01-01
I Zusman, B Sandler, P Gurevich, R Zusman, P Smirnoff, Y Tendler, D Bass, A Shani, E Idelevich, R Pfefferman, B Davidovich, M Huszar, J Glick
{"title":"Comparative study of the role of serum levels of p53 antigen and its tumor cell concentration in colon cancer detection.","authors":"I Zusman,&nbsp;B Sandler,&nbsp;P Gurevich,&nbsp;R Zusman,&nbsp;P Smirnoff,&nbsp;Y Tendler,&nbsp;D Bass,&nbsp;A Shani,&nbsp;E Idelevich,&nbsp;R Pfefferman,&nbsp;B Davidovich,&nbsp;M Huszar,&nbsp;J Glick","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>The role of serum levels of p53 antigen in detection of colon cancer was studied in different groups of cancer and noncancer patients and was compared with the results of immunohistochemical analyses. The p53 antigen was isolated from the human serum as a cytoplasmic fraction using the recently described new type of columns for affinity chromatography, gel fiberglass columns (Zusman and Zusman, 1995). Its concentration was detected by high performance liquid chromatography. The serum level of the p53 antigen significantly increased in cancer patients (3.6 mg ml(-1)) as compared to its concentration in patients with benign tumors (1.7 mg ml(-1)) or in patients with noncancer disorders (0.49 mg ml(-1)), and this was found to be a result of higher concentration of p53 protein in tumor cells. Coefficient of correlation between cellular concentration of p53 protein and its serum level was 0.44 in noncancer lesions and 0.48 in cancer patients. Serum levels of p53 antigen was shown to be highly active either in patients with noncancer lesions or in patients with cancer (r = 0.46 and 0.51 respectively), whereas the cell determination of p53 protein was effective only among noncancer patients (r = 0.61) but not in cancer patients (r = 0.22). The findings suggests that serum determination of p53 antigen can perhaps reveal this oncoprotein already in the early stages of cancer or even predict the putative development of cancer. The possibility to use the serum-levels of p53 antigen in the follow up patients with chronic diseases and to detect transformation of these diseases into cancer, or monitoring former cancer patients in order to detect as early as possible the incidence of recurrent cancer is discussed.</p>","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 3","pages":"123-8"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20013646","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Evidence for restricted diversity of antigen-specific human antibodies in immunized hu-PBL-SCID mice. 免疫hu-PBL-SCID小鼠中抗原特异性人抗体有限多样性的证据。
Human antibodies and hybridomas Pub Date : 1996-01-01
R Bazin, M C Chevrier, R Delage, R Lemieux
{"title":"Evidence for restricted diversity of antigen-specific human antibodies in immunized hu-PBL-SCID mice.","authors":"R Bazin,&nbsp;M C Chevrier,&nbsp;R Delage,&nbsp;R Lemieux","doi":"","DOIUrl":"","url":null,"abstract":"<p><p>Previous studies have revealed that specific human humoral immune responses could be produced in immunized SCID mice after engraftment of human lymphocytes (hu-PBL-SCID). On the other hand, the engrafted repertoire of B cell clones is known to be skewed in hu-PBL-SCID with the corresponding production of only a limited set of major human antibodies. In this work, we have analyzed the diversity of tetanus toxoid-specific human antibodies produced in immunized hu-PBL-SCID mice in comparison with the total serum antibody population using zone electrophoresis followed by blotting. The results showed that the diversity of tetanus toxoid-specific antibody population was more restricted than that of the total human antibody population, with some animal sera containing a single band of tetanus toxoid-specific antibody molecule, in clear contrast to the polyclonal response of the PBL donor. Absorption experiments showed tetanus toxoid-specific antibodies could account for a significant proportion (up to 10%) of the total human antibodies present in hu-PBL-SCID mouse sera. The inability to expand a high number of different antigen-specific B cell clones in immunized hu-PBL-SCID mice represents an important intrinsic limitation of this animal model which may be caused by defects in T cell help.</p>","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 3","pages":"129-34"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"20013647","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Lung cancer-reacting human recombinant antibody AE6F4: potential usefulness in the sputum cytodiagnosis. 肺癌反应的人重组抗体AE6F4:在痰细胞诊断中的潜在用途。
Human antibodies and hybridomas Pub Date : 1996-01-01 DOI: 10.3233/HAB-1996-7104
M. Shoji, S. Kawamoto, K. Seki, K. Teruya, Y. Setoguchi, K. Mochizuki, M. Kato, S. Hashizume, T. Hanagiri, T. Yoshimatsu, K. Nakanishi, K. Yasumoto, A. Nagashima, H. Nakahashi, T. Suzuki, T. Imai, S. Shirahata, K. Nomoto, H. Murakami
{"title":"Lung cancer-reacting human recombinant antibody AE6F4: potential usefulness in the sputum cytodiagnosis.","authors":"M. Shoji, S. Kawamoto, K. Seki, K. Teruya, Y. Setoguchi, K. Mochizuki, M. Kato, S. Hashizume, T. Hanagiri, T. Yoshimatsu, K. Nakanishi, K. Yasumoto, A. Nagashima, H. Nakahashi, T. Suzuki, T. Imai, S. Shirahata, K. Nomoto, H. Murakami","doi":"10.3233/HAB-1996-7104","DOIUrl":"https://doi.org/10.3233/HAB-1996-7104","url":null,"abstract":"Human monoclonal antibody (hMAb) AE6F4 has been shown to be potentially useful for immunocytological detection of lung cancer cells in sputum. By recombinant DNA technology, IgM type hMAb AE6F4 was switched to lgG. The IgG mimic recombinant AE6F4 antibody expression plasmid was assembled using the antibody heavy chain gene, which ligated the gene encoding VH and CH1(mu) domains of hMAb AE6F4 heavy chain to the gene encoding CH2(gamma 1) and CH3(gamma 1) domains of human IgG heavy chain, and the antibody light chain gene of hMAb AE6F4. The recombinant antibody expressed by baby hamster kidney (BHK)-21 cells showed molecular size equivalence to IgG, and consisted of human mu-gamma hybrid heavy and kappa light chains. The immunological specificity of the recombinant antibody was the same as that of hMAb AE6F4 by immunoblotting analysis to the 14-3-3 protein, the putative antigen of hMAb AE6F4, and by immunohistochemical and immunocytological analyses using tissue sections and sputa of lung cancer patients. The transfected BHK-21 cells produced the recombinant antibody persistently and the productivity was greater than 20 times that by human-human hybridoma producing hMAb AE6F4.","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 1 1","pages":"27-36"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/HAB-1996-7104","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69906100","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 8
A rapid method for purification of monoclonal human IgM from mass culture. 一种快速从大众培养中纯化人IgM单克隆的方法。
Human antibodies and hybridomas Pub Date : 1996-01-01 DOI: 10.3233/HAB-1996-7105
H. Vollmers, E. Woźniak, Ewa Stepien-Bötsch, U. Zimmermann, H. Müller-hermelink
{"title":"A rapid method for purification of monoclonal human IgM from mass culture.","authors":"H. Vollmers, E. Woźniak, Ewa Stepien-Bötsch, U. Zimmermann, H. Müller-hermelink","doi":"10.3233/HAB-1996-7105","DOIUrl":"https://doi.org/10.3233/HAB-1996-7105","url":null,"abstract":"We describe in this paper the rapid and cheap purification of human immunoglobulin M from hybridoma supernatant of mass culture. The method consists of two steps: 1. concentration of supernatant by ultrafiltration and 2. dialysis against distilled water, pH 6.4. To produce the supernatant, the hybridomas are grown in RPMI media with fetal calf serum (10% FCS) in 250 ml flasks under normal tissue culture conditions. More than 14 mg IgM can be nearly selectively purified within 6 h from 5 l of antibody containing hybridoma supernatant. Most of the IgM molecules stay in a penta- and monomeric form and are positive in physiological and immunohistochemical studies.","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 1 1","pages":"37-41"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/HAB-1996-7105","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69906148","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 12
Reactivity to tyrosinase: expression in cancer (melanoma) and autoimmunity (vitiligo). 对酪氨酸酶的反应性:在癌症(黑色素瘤)和自身免疫(白癜风)中的表达。
Human antibodies and hybridomas Pub Date : 1996-01-01 DOI: 10.3233/HAB-1996-7402
O. Merimsky, Y. Shoenfeld, E. Baharav, R. Zigelman, P. Fishman
{"title":"Reactivity to tyrosinase: expression in cancer (melanoma) and autoimmunity (vitiligo).","authors":"O. Merimsky, Y. Shoenfeld, E. Baharav, R. Zigelman, P. Fishman","doi":"10.3233/HAB-1996-7402","DOIUrl":"https://doi.org/10.3233/HAB-1996-7402","url":null,"abstract":"Anti-tyrosinase antibodies are found in the sera of patients with diffuse vitiligo, metastatic melanoma and in sera of patients with melanoma and hypopigmentation (MAH). The autoantigen is tyrosinase itself, the enzyme that participates in pigment (melanin) formation by both melanocytes and melanoma cells. The production of autoantibodies in both diseases is associated with the development of white patches on the patients' skin. The presence of these autoantibodies in patients with melanoma may suggest a better prognosis. Cross-antigenicity between melanoma cells and normal melanocytes is most probably the key mechanism leading to the appearance of MAH. Anti-tyrosinase antibodies are absorbed by melanocytes and by melanoma cells in all the 3 situations (melanoma, vitiligo, MAH). However, since the production of antibodies in vitiligo exceeds that in melanoma or MAH, the antibodies are detected in significantly higher levels only in vitiligo. It is suggested here that anti-tyrosinase antibodies may be responsible, or at least participate in destruction of normal melanocytes during the immune response to melanoma antigens. This mechanism may be responsible for the phenomenon of MAH in patients with melanoma, and for the formation of the autoimmune vitiligo. Anti-tyrosinase antibodies may serve for two clinical applications. One is a marker for monitoring and follow up of patients with melanoma treated by immune therapy. The second is active (or passive) immunotherapy. We have recently shown that C57BL/6J mice immunized with tyrosinase generated a high titer of antityrosinase antibodies, and following the inoculation of melanoma cells developed lower number of lung metastases, compared to the unvaccinated control group.","PeriodicalId":77166,"journal":{"name":"Human antibodies and hybridomas","volume":"7 4 1","pages":"151-6"},"PeriodicalIF":0.0,"publicationDate":"1996-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.3233/HAB-1996-7402","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"69906792","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 22
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