T. Reinard et al., BIOCHEMICAL-PROPERTIES OF A NOVEL CELL-WALL PROTEIN ASSOCIATED WITH ELONGATION GROWTH IN HIGHER-PLANTS, Journal of Experimental Botany, 45(280), 1994, pp. 1593-1601
A monoclonal antibody of IgM-type (TIM-11B2) was screened from a hybri
doma library. The antibody recognizes a 40 kDa glycoprotein, p40, with
high specificity. This protein was detected in all plant species exam
ined so far and was found to be located both solubly and ionically-bou
nd within the primary cell wall.The strongest immunobiochemical signal
s of p40 were found in tissues undergoing elongation growth, whereas i
n other tissues only a faint signal could be detected. Those included
the non-elongating parts of different seedlings, such as the apical pa
rt of monocot primary leaves or the leaves of dicots grown in tight. I
nhibition of pea epicotyl growth by white light irradiation resulted i
n a strong decrease of the immunostain signal. On the other hand, indu
ction of rapid coleoptile growth in rice seedlings induced by submerge
nce resulted in a strong increase of the immunobiochemical signal of p
40. Time-course studies on the expression of p40 during protoplast reg
eneration revealed that p40 is apparently not involved in cell wall fo
rmation. The hypothesis that p40 is characteristic for tissues with th
e ability for elongation growth is discussed. Comparison of biochemica
l data and location of p40 with proteins described up to now indicate
that this glycoprotein has not been characterized before.