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[Passive immunity by splenocyte transfer against amebic meningoencephalitis in mice].

Kisaengch'unghak chapchi. The Korean journal of parasitology

Im KI, Ryu JS.
PMID: 12811044
Kisaengchunghak Chapchi. 1988 Sep;26(3):169-173. doi: 10.3347/kjp.1988.26.3.169.

The role of passive cell-mediated transfer of immunity against primary amoebic meningoencephalitis(PAME) in mice was studied. Naegleria fowleri, ITMAP 359, were cultured in CGVS medium. The ICR mice used were six week-old males of average weight of 15 g....

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Im KI, Ryu JS. [Passive immunity by splenocyte transfer against amebic meningoencephalitis in mice]. Kisaengchunghak Chapchi. 1988;26(3):169-173doi: 10.3347/kjp.1988.26.3.169.
Im, K. I., & Ryu, J. S. (1988). [Passive immunity by splenocyte transfer against amebic meningoencephalitis in mice]. Kisaengch'unghak chapchi. The Korean journal of parasitology, 26(3), 169-173. https://doi.org/10.3347/kjp.1988.26.3.169
Im, Kyung Il, and Ryu, Jae Sook. "[Passive immunity by splenocyte transfer against amebic meningoencephalitis in mice]." Kisaengch'unghak chapchi. The Korean journal of parasitology vol. 26,3 (1988): 169-173. doi: https://doi.org/10.3347/kjp.1988.26.3.169
Im KI, Ryu JS. [Passive immunity by splenocyte transfer against amebic meningoencephalitis in mice]. Kisaengchunghak Chapchi. 1988 Sep;26(3):169-173. doi: 10.3347/kjp.1988.26.3.169. Korean. PMID: 12811044.
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Identification of Hemagglutinin of Jack Bean with Concanavalin A.

Journal of bacteriology

Sumner JB, Howell SF.
PMID: 16559945
J Bacteriol. 1936 Aug;32(2):227-37. doi: 10.1128/jb.32.2.227-237.1936.

No abstract available.

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Sumner JB, Howell SF. Identification of Hemagglutinin of Jack Bean with Concanavalin A. J Bacteriol. 1936;32(2):227-37doi: 10.1128/jb.32.2.227-237.1936.
Sumner, J. B., & Howell, S. F. (1936). Identification of Hemagglutinin of Jack Bean with Concanavalin A. Journal of bacteriology, 32(2), 227-37. https://doi.org/10.1128/jb.32.2.227-237.1936
Sumner, J B, and Howell, S F. "Identification of Hemagglutinin of Jack Bean with Concanavalin A." Journal of bacteriology vol. 32,2 (1936): 227-37. doi: https://doi.org/10.1128/jb.32.2.227-237.1936
Sumner JB, Howell SF. Identification of Hemagglutinin of Jack Bean with Concanavalin A. J Bacteriol. 1936 Aug;32(2):227-37. doi: 10.1128/jb.32.2.227-237.1936. PMID: 16559945; PMCID: PMC543784.
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Development of mouse embryos in media containing lectins.

Theriogenology

Menino AR, Williams JS, Gardiner CS.
PMID: 16726597
Theriogenology. 1989 Apr;31(4):821-34. doi: 10.1016/0093-691x(89)90027-7.

Lectins known to stimulate mitosis in cultured cells were evaluated for effects on development of mouse embryos in vitro. Two-cell mouse embryos were cultured in one of the following treatments: Whitten's medium as the control medium; Whitten's medium with...

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Menino AR, Williams JS, Gardiner CS. Development of mouse embryos in media containing lectins. Theriogenology. 1989;31(4):821-34doi: 10.1016/0093-691x(89)90027-7.
Menino, A. R., Williams, J. S., & Gardiner, C. S. (1989). Development of mouse embryos in media containing lectins. Theriogenology, 31(4), 821-34. https://doi.org/10.1016/0093-691x(89)90027-7
Menino, A R, et al. "Development of mouse embryos in media containing lectins." Theriogenology vol. 31,4 (1989): 821-34. doi: https://doi.org/10.1016/0093-691x(89)90027-7
Menino AR, Williams JS, Gardiner CS. Development of mouse embryos in media containing lectins. Theriogenology. 1989 Apr;31(4):821-34. doi: 10.1016/0093-691x(89)90027-7. PMID: 16726597.
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Sugar-sensitive thin films composed of concanavalin A and glycogen.

Analytical sciences : the international journal of the Japan Society for Analytical Chemistry

Sato K, Imoto Y, Sugama J, Seki S, Inoue H, Odagiri T, Anzai J.
PMID: 15478330
Anal Sci. 2004 Sep;20(9):1247-8. doi: 10.2116/analsci.20.1247.

Sugar-sensitive thin films were prepared by a layer-by-layer deposition of concanavalin A (Con A) and glycogen on the surface of a quartz slide and their sugar-induced decomposition was studied. The Con A/glycogen multilayer films can be decomposed by exposing...

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Sato K, Imoto Y, Sugama J, et al. Sugar-sensitive thin films composed of concanavalin A and glycogen. Anal Sci. 2004;20(9):1247-8doi: 10.2116/analsci.20.1247.
Sato, K., Imoto, Y., Sugama, J., Seki, S., Inoue, H., Odagiri, T., & Anzai, J. (2004). Sugar-sensitive thin films composed of concanavalin A and glycogen. Analytical sciences : the international journal of the Japan Society for Analytical Chemistry, 20(9), 1247-8. https://doi.org/10.2116/analsci.20.1247
Sato, Katsuhiko, et al. "Sugar-sensitive thin films composed of concanavalin A and glycogen." Analytical sciences : the international journal of the Japan Society for Analytical Chemistry vol. 20,9 (2004): 1247-8. doi: https://doi.org/10.2116/analsci.20.1247
Sato K, Imoto Y, Sugama J, Seki S, Inoue H, Odagiri T, Anzai J. Sugar-sensitive thin films composed of concanavalin A and glycogen. Anal Sci. 2004 Sep;20(9):1247-8. doi: 10.2116/analsci.20.1247. PMID: 15478330.
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Functionalization of single-walled carbon nanotube by the covalent modification with polymer chains.

Journal of colloid and interface science

Kitano H, Tachimoto K, Anraku Y.
PMID: 17095004
J Colloid Interface Sci. 2007 Feb 01;306(1):28-33. doi: 10.1016/j.jcis.2006.10.034. Epub 2006 Oct 24.

A single-walled carbon nanotube (SWNT), which had been oxidized by incubation with a mixture of nitric acid and sulfuric acid to afford carboxyl groups at its ends, was incubated with an azo-type radical initiator carrying poly(2-methacryloyloxyethyl D-glucopyranoside) blocks at...

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Kitano H, Tachimoto K, Anraku Y. Functionalization of single-walled carbon nanotube by the covalent modification with polymer chains. J Colloid Interface Sci. 2006;306(1):28-33doi: 10.1016/j.jcis.2006.10.034.
Kitano, H., Tachimoto, K., & Anraku, Y. (2007). Functionalization of single-walled carbon nanotube by the covalent modification with polymer chains. Journal of colloid and interface science, 306(1), 28-33. https://doi.org/10.1016/j.jcis.2006.10.034
Kitano, Hiromi, et al. "Functionalization of single-walled carbon nanotube by the covalent modification with polymer chains." Journal of colloid and interface science vol. 306,1 (2007): 28-33. doi: https://doi.org/10.1016/j.jcis.2006.10.034
Kitano H, Tachimoto K, Anraku Y. Functionalization of single-walled carbon nanotube by the covalent modification with polymer chains. J Colloid Interface Sci. 2007 Feb 01;306(1):28-33. doi: 10.1016/j.jcis.2006.10.034. Epub 2006 Oct 24. PMID: 17095004.
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The C-S Lyases of Higher Plants : Direct Comparison of the Physical Properties of Homogeneous Alliin Lyase of Garlic (Allium sativum) and Onion (Allium cepa).

Plant physiology

Nock LP, Mazelis M.
PMID: 16665807
Plant Physiol. 1987 Dec;85(4):1079-83. doi: 10.1104/pp.85.4.1079.

Garlic and onion alliin lyases, although from closely related species, have many differences. The two enzymes differ in their K(m) values, pH optima, and isoelectric points. There is a major difference in their molecular weight and subunit structure. The...

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Nock LP, Mazelis M. The C-S Lyases of Higher Plants : Direct Comparison of the Physical Properties of Homogeneous Alliin Lyase of Garlic (Allium sativum) and Onion (Allium cepa). Plant Physiol. 1987;85(4):1079-83doi: 10.1104/pp.85.4.1079.
Nock, L. P., & Mazelis, M. (1987). The C-S Lyases of Higher Plants : Direct Comparison of the Physical Properties of Homogeneous Alliin Lyase of Garlic (Allium sativum) and Onion (Allium cepa). Plant physiology, 85(4), 1079-83. https://doi.org/10.1104/pp.85.4.1079
Nock, L P, and Mazelis, M. "The C-S Lyases of Higher Plants : Direct Comparison of the Physical Properties of Homogeneous Alliin Lyase of Garlic (Allium sativum) and Onion (Allium cepa)." Plant physiology vol. 85,4 (1987): 1079-83. doi: https://doi.org/10.1104/pp.85.4.1079
Nock LP, Mazelis M. The C-S Lyases of Higher Plants : Direct Comparison of the Physical Properties of Homogeneous Alliin Lyase of Garlic (Allium sativum) and Onion (Allium cepa). Plant Physiol. 1987 Dec;85(4):1079-83. doi: 10.1104/pp.85.4.1079. PMID: 16665807; PMCID: PMC1054397.
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Tonoplast vesicles of opposite sidedness from soybean hypocotyls by preparative free-flow electrophoresis.

Plant physiology

Canut H, Brightman A, Boudet AM, Morré DJ.
PMID: 16667810
Plant Physiol. 1990 Nov;94(3):1149-56. doi: 10.1104/pp.94.3.1149.

Tonoplast vesicles were purified from a microsomal fraction isolated from etiolated soybean hypocotyls (Glycine max L.) by preparative free-flow electrophoresis. Marker enzyme determinations and immunoblot analysis against the vacuolar-ATPase confirmed the nature and the purity of the isolated membranes....

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Canut H, Brightman A, Boudet AM, et al. Tonoplast vesicles of opposite sidedness from soybean hypocotyls by preparative free-flow electrophoresis. Plant Physiol. 1990;94(3):1149-56doi: 10.1104/pp.94.3.1149.
Canut, H., Brightman, A., Boudet, A. M., & Morré, D. J. (1990). Tonoplast vesicles of opposite sidedness from soybean hypocotyls by preparative free-flow electrophoresis. Plant physiology, 94(3), 1149-56. https://doi.org/10.1104/pp.94.3.1149
Canut, H, et al. "Tonoplast vesicles of opposite sidedness from soybean hypocotyls by preparative free-flow electrophoresis." Plant physiology vol. 94,3 (1990): 1149-56. doi: https://doi.org/10.1104/pp.94.3.1149
Canut H, Brightman A, Boudet AM, Morré DJ. Tonoplast vesicles of opposite sidedness from soybean hypocotyls by preparative free-flow electrophoresis. Plant Physiol. 1990 Nov;94(3):1149-56. doi: 10.1104/pp.94.3.1149. PMID: 16667810; PMCID: PMC1077355.
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The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum.

Plant physiology

Hankins CN, Herman EM, Kindinger J, Shannon LM.
PMID: 16668191
Plant Physiol. 1991 May;96(1):98-103. doi: 10.1104/pp.96.1.98.

The seeds of Spartium junceum contained a large quantity of lectin-like protein that did not appear to be either a hemagglutinin or active lectin. The cross-reactive material (CRM), like most legume seed lectins, was a tetrameric glycoprotein of about...

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Hankins CN, Herman EM, Kindinger J, et al. The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum. Plant Physiol. 1991;96(1):98-103doi: 10.1104/pp.96.1.98.
Hankins, C. N., Herman, E. M., Kindinger, J., & Shannon, L. M. (1991). The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum. Plant physiology, 96(1), 98-103. https://doi.org/10.1104/pp.96.1.98
Hankins, C N, et al. "The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum." Plant physiology vol. 96,1 (1991): 98-103. doi: https://doi.org/10.1104/pp.96.1.98
Hankins CN, Herman EM, Kindinger J, Shannon LM. The Purification, Properties, and Localization of an Abundant Legume Seed Lectin Cross-Reactive Material from Spartium junceum. Plant Physiol. 1991 May;96(1):98-103. doi: 10.1104/pp.96.1.98. PMID: 16668191; PMCID: PMC1080718.
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The Glycoproteins of Plant Seeds : ANALYSIS BY TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS AND BY THEIR LECTIN-BINDING PROPERTIES.

Plant physiology

Basha SM, Roberts RM.
PMID: 16661796
Plant Physiol. 1981 May;67(5):936-9. doi: 10.1104/pp.67.5.936.

Protein from the jack bean, peanut, soybean and kidney bean seeds were extracted with a solution containing 9.3 molar urea, 5 millimolar K(2)CO(3), 0.5% dithiothreitol and 2% Nonidet P-40 and then subjected to two-dimensional gel electrophoresis. After electrophoresis, the...

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Basha SM, Roberts RM. The Glycoproteins of Plant Seeds : ANALYSIS BY TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS AND BY THEIR LECTIN-BINDING PROPERTIES. Plant Physiol. 1981;67(5):936-9doi: 10.1104/pp.67.5.936.
Basha, S. M., & Roberts, R. M. (1981). The Glycoproteins of Plant Seeds : ANALYSIS BY TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS AND BY THEIR LECTIN-BINDING PROPERTIES. Plant physiology, 67(5), 936-9. https://doi.org/10.1104/pp.67.5.936
Basha, S M, and Roberts, R M. "The Glycoproteins of Plant Seeds : ANALYSIS BY TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS AND BY THEIR LECTIN-BINDING PROPERTIES." Plant physiology vol. 67,5 (1981): 936-9. doi: https://doi.org/10.1104/pp.67.5.936
Basha SM, Roberts RM. The Glycoproteins of Plant Seeds : ANALYSIS BY TWO-DIMENSIONAL POLYACRYLAMIDE GEL ELECTROPHORESIS AND BY THEIR LECTIN-BINDING PROPERTIES. Plant Physiol. 1981 May;67(5):936-9. doi: 10.1104/pp.67.5.936. PMID: 16661796; PMCID: PMC425804.
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Vacuoles from Sugarcane Suspension Cultures : I. ISOLATION AND PARTIAL CHARACTERIZATION.

Plant physiology

Thom M, Maretzki A, Komor E.
PMID: 16662393
Plant Physiol. 1982 Jun;69(6):1315-9. doi: 10.1104/pp.69.6.1315.

Vacuoles were isolated from suspension cultures of sugarcane (Saccharum sp.) cells by centrifugation of protoplasts at high g force against a 12% (w/v) Ficoll solution. Distribution of marker enzymes and Concanavalin A binding showed an 11% contamination of the...

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Thom M, Maretzki A, Komor E. Vacuoles from Sugarcane Suspension Cultures : I. ISOLATION AND PARTIAL CHARACTERIZATION. Plant Physiol. 1982;69(6):1315-9doi: 10.1104/pp.69.6.1315.
Thom, M., Maretzki, A., & Komor, E. (1982). Vacuoles from Sugarcane Suspension Cultures : I. ISOLATION AND PARTIAL CHARACTERIZATION. Plant physiology, 69(6), 1315-9. https://doi.org/10.1104/pp.69.6.1315
Thom, M, et al. "Vacuoles from Sugarcane Suspension Cultures : I. ISOLATION AND PARTIAL CHARACTERIZATION." Plant physiology vol. 69,6 (1982): 1315-9. doi: https://doi.org/10.1104/pp.69.6.1315
Thom M, Maretzki A, Komor E. Vacuoles from Sugarcane Suspension Cultures : I. ISOLATION AND PARTIAL CHARACTERIZATION. Plant Physiol. 1982 Jun;69(6):1315-9. doi: 10.1104/pp.69.6.1315. PMID: 16662393; PMCID: PMC426408.
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Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine.

Plant physiology

Hori H, Kaushal GP, Elbein AD.
PMID: 16664119
Plant Physiol. 1985 Mar;77(3):687-94. doi: 10.1104/pp.77.3.687.

Cultures of soybean cells incorporate [5,6-(3)H]-l-fucose into various cellular components including lipids and proteins. The membrane glyco-proteins were digested with pronase to produce glycopeptides, and the glycopeptides were isolated on columns of Biogel P-4. The major fucoselabeled glycopeptide sized...

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Hori H, Kaushal GP, Elbein AD. Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant Physiol. 1985;77(3):687-94doi: 10.1104/pp.77.3.687.
Hori, H., Kaushal, G. P., & Elbein, A. D. (1985). Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant physiology, 77(3), 687-94. https://doi.org/10.1104/pp.77.3.687
Hori, H, et al. "Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine." Plant physiology vol. 77,3 (1985): 687-94. doi: https://doi.org/10.1104/pp.77.3.687
Hori H, Kaushal GP, Elbein AD. Fucosylation of membrane proteins in soybean cultured cells : effects of tunicamycin and swainsonine. Plant Physiol. 1985 Mar;77(3):687-94. doi: 10.1104/pp.77.3.687. PMID: 16664119; PMCID: PMC1064585.
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Wheat invertases : characterization of cell wall-bound and soluble forms.

Plant physiology

Krishnan HB, Blanchette JT, Okita TW.
PMID: 16664223
Plant Physiol. 1985 Jun;78(2):241-5. doi: 10.1104/pp.78.2.241.

Wheat coleoptiles have two distinct invertases, a soluble and a cell wall-bound form as indicated by results from cytochemical and biochemical studies. These enzyme activities differ in their pH optima, chromatographic behavior on diethylaminoethyl cellulose, kinetic properties, thermal stability,...

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Krishnan HB, Blanchette JT, Okita TW. Wheat invertases : characterization of cell wall-bound and soluble forms. Plant Physiol. 1985;78(2):241-5doi: 10.1104/pp.78.2.241.
Krishnan, H. B., Blanchette, J. T., & Okita, T. W. (1985). Wheat invertases : characterization of cell wall-bound and soluble forms. Plant physiology, 78(2), 241-5. https://doi.org/10.1104/pp.78.2.241
Krishnan, H B, et al. "Wheat invertases : characterization of cell wall-bound and soluble forms." Plant physiology vol. 78,2 (1985): 241-5. doi: https://doi.org/10.1104/pp.78.2.241
Krishnan HB, Blanchette JT, Okita TW. Wheat invertases : characterization of cell wall-bound and soluble forms. Plant Physiol. 1985 Jun;78(2):241-5. doi: 10.1104/pp.78.2.241. PMID: 16664223; PMCID: PMC1064712.
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