Type-I-hypersensitivity to 15 kDa, 28 kDa and 54 kDa proteins in vitellogenin specific to Gadus chalcogrammus roe
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منابع مشابه
purification and identification of 72 kda and 15 kda allergens from broussonetia papyrifera pollen.
“broussonetia papyrifera” (chinese mulberry) pollen is an important source of allergens in regions surrounding shanghai, china. to identify and purify major allergens from “b. papyrifera” pollen that reacted with serum antibodies from sensitized patients, “b. papyrifera” pollen was defatted, dried, and extracted proteins were separated using sp cationic exchange or q anionic exchange columns. s...
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We have previously identified a 15-kDa interferon-induced protein that is recognized by affinity-purified rabbit polyclonal antibodies against ubiquitin (Haas, A. L., Ahrens, P., Bright, P. M., and Ankel, H. (1987) J. Biol. Chem. 262, 11315-11323). This ubiquitin cross-reactive protein (UCRP) possesses significant homology to a tandem diubiquitin sequence. Since the biological effects of ubiqui...
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Two major gelatinolytic metalloproteinases (gelatinases) of 65 kDa and 92 kDa were purified from a tumor cell line. Analysis of collagen degradation showed that native full-length Engelbreth-Holm-Swarm (EHS) type IV collagen was not cleaved by the purified gelatinases under conditions where native pepsin-extracted human placental type IV and V collagen and heat-denatured collagens were markedly...
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Description MMP2 is a Zn dependent endopeptidase, synthesized and secreted in zymogen form. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide'pro' domain that maintains enzyme-latency until cleaved or disrupted, and a catalytic domain that contains the conserved zin...
متن کاملMMP 9 ( matrix metallopeptidase 9 ( gelatinase B , 92 kDa gelatinase , 92 kDa type IV collagenase ) )
MMP-9 is a Zn+2 dependent endopeptidase, synthesized and secreted in monomeric form as zymogen. The structure is almost similar to MMP2, another member of matrixmetalloproteinase family. The nascent form of the protein shows an N-terminal signal sequence ('pre' domain) that directs the protein to the endoplasmic reticulum. The pre domain is followed by a propeptide-'pro' domain that maintains e...
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ژورنال
عنوان ژورنال: Allergology International
سال: 2020
ISSN: 1323-8930
DOI: 10.1016/j.alit.2019.09.007