A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo

Deborah P. Delmer; M. Volokita; M. Solomon; U. Fritz; W. Delphendahl; W. Herth

doi:10.1007/BF01378937

A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo

Deborah P. Delmer, M. Volokita, M. Solomon, U. Fritz, W. Delphendahl, W. Herth^*

^*Corresponding author for this work

Alexander Silberman Institute of Life Sciences

Research output: Contribution to journal › Article › peer-review

41 Scopus citations

Abstract

A monoclonal antibody (MAb) capable of immobilizing detergent-solubilized UDP-glucose: (1→3)-β-glucan (callose) synthase activity from higher plants has been selected and characterized. On Western blots this MAb recognizes a polypeptide of about 65 kDa found in membranes isolated from a variety of plant sources. The polypeptide recognized by this MAb does not appear to bind the substrate UDP-glucose, and evidence is presented which indicates that this polypeptide associates with the enzyme complex in a cation-dependent manner under conditions where the callose synthase assumes a larger size. Indirect immunofluorescence localization with this MAb was positive with sieve plates of cucumber (Cucumis sativus) seedlings, and with plasmodesmata of onion (Allium cepa) epidermal cells, both being sites of localized, stress-induced callose deposition.

Original language	English
Pages (from-to)	33-42
Number of pages	10
Journal	Protoplasma
Volume	176
Issue number	1-2
DOIs	https://doi.org/10.1007/BF01378937
State	Published - Mar 1993

Keywords

65 kDa polypeptide
Callose
Enzyme immobilization
Immunofluorescence
Monoclonal antibody
β-1,3-Glucan synthase complex

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Delmer, D. P., Volokita, M., Solomon, M., Fritz, U., Delphendahl, W., & Herth, W. (1993). A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo. Protoplasma, 176(1-2), 33-42. https://doi.org/10.1007/BF01378937

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title = "A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo",

abstract = "A monoclonal antibody (MAb) capable of immobilizing detergent-solubilized UDP-glucose: (1→3)-β-glucan (callose) synthase activity from higher plants has been selected and characterized. On Western blots this MAb recognizes a polypeptide of about 65 kDa found in membranes isolated from a variety of plant sources. The polypeptide recognized by this MAb does not appear to bind the substrate UDP-glucose, and evidence is presented which indicates that this polypeptide associates with the enzyme complex in a cation-dependent manner under conditions where the callose synthase assumes a larger size. Indirect immunofluorescence localization with this MAb was positive with sieve plates of cucumber (Cucumis sativus) seedlings, and with plasmodesmata of onion (Allium cepa) epidermal cells, both being sites of localized, stress-induced callose deposition.",

keywords = "65 kDa polypeptide, Callose, Enzyme immobilization, Immunofluorescence, Monoclonal antibody, β-1,3-Glucan synthase complex",

author = "Delmer, {Deborah P.} and M. Volokita and M. Solomon and U. Fritz and W. Delphendahl and W. Herth",

year = "1993",

month = mar,

doi = "10.1007/BF01378937",

language = "אנגלית",

volume = "176",

pages = "33--42",

journal = "Protoplasma",

issn = "0033-183X",

publisher = "Springer",

number = "1-2",

}

Delmer, DP, Volokita, M, Solomon, M, Fritz, U, Delphendahl, W & Herth, W 1993, 'A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo', Protoplasma, vol. 176, no. 1-2, pp. 33-42. https://doi.org/10.1007/BF01378937

A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo. / Delmer, Deborah P.; Volokita, M.; Solomon, M. et al.
In: Protoplasma, Vol. 176, No. 1-2, 03.1993, p. 33-42.

Research output: Contribution to journal › Article › peer-review

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T1 - A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo

AU - Delmer, Deborah P.

AU - Volokita, M.

AU - Solomon, M.

AU - Fritz, U.

AU - Delphendahl, W.

AU - Herth, W.

PY - 1993/3

Y1 - 1993/3

N2 - A monoclonal antibody (MAb) capable of immobilizing detergent-solubilized UDP-glucose: (1→3)-β-glucan (callose) synthase activity from higher plants has been selected and characterized. On Western blots this MAb recognizes a polypeptide of about 65 kDa found in membranes isolated from a variety of plant sources. The polypeptide recognized by this MAb does not appear to bind the substrate UDP-glucose, and evidence is presented which indicates that this polypeptide associates with the enzyme complex in a cation-dependent manner under conditions where the callose synthase assumes a larger size. Indirect immunofluorescence localization with this MAb was positive with sieve plates of cucumber (Cucumis sativus) seedlings, and with plasmodesmata of onion (Allium cepa) epidermal cells, both being sites of localized, stress-induced callose deposition.

AB - A monoclonal antibody (MAb) capable of immobilizing detergent-solubilized UDP-glucose: (1→3)-β-glucan (callose) synthase activity from higher plants has been selected and characterized. On Western blots this MAb recognizes a polypeptide of about 65 kDa found in membranes isolated from a variety of plant sources. The polypeptide recognized by this MAb does not appear to bind the substrate UDP-glucose, and evidence is presented which indicates that this polypeptide associates with the enzyme complex in a cation-dependent manner under conditions where the callose synthase assumes a larger size. Indirect immunofluorescence localization with this MAb was positive with sieve plates of cucumber (Cucumis sativus) seedlings, and with plasmodesmata of onion (Allium cepa) epidermal cells, both being sites of localized, stress-induced callose deposition.

KW - 65 kDa polypeptide

KW - Callose

KW - Enzyme immobilization

KW - Immunofluorescence

KW - Monoclonal antibody

KW - β-1,3-Glucan synthase complex

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A monoclonal antibody recognizes a 65 kDa higher plant membrane polypeptide which undergoes cation-dependent association with callose synthase in vitro and co-localizes with sites of high callose deposition in vivo

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Keywords

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