کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
9474537 | 1322383 | 2005 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Specificity of action of an insect proteinase purified from wheat grain infested by the New Zealand wheat bug, Nysius huttoni
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
علوم زراعت و اصلاح نباتات
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
A salivary proteinase from the New Zealand wheat bug (Nysius huttoni) was partially purified and analysed for substrate specificity by a variety of techniques on the following proteins: wheat, rye, barley and corn proteins, haemoglobin, bovine serum albumin, cytochrome c, cytochrome c oxidase, elastin, collagen, gelatine, keratin (hide powder), fibrin, azo-casein, α-casein, β-casein and κ-casein. The only proteins substantially hydrolysed (> 50%) by Nysius-proteinase were the high Mr glutenin subunits of wheat, the high Mr secalin and Mr 60,000 γ-secalin of rye, the d-hordeins of barley, the Mr 70,000, Mr 66,000 and Mr 58,000 C hordeins, and β-casein subunit of bovine milk. Sequence analysis of the peptide products of enzyme reaction on high Mr glutenin subunits, β-casein and κ-casein revealed that glutamine occupied the P1 position relative to the scissile bond at all cleavage sites. Proline in the P3 or P4 position, and particular residues in the Pâ²1 position relative to the scissile bond may also be preferred structural features. A variety of fluorogenic substrates made from synthetic peptides with glutamine in the P1 position relative to the fluorogenic group were tested with the enzyme, but none reacted.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Cereal Science - Volume 42, Issue 2, September 2005, Pages 185-191
Journal: Journal of Cereal Science - Volume 42, Issue 2, September 2005, Pages 185-191
نویسندگان
D. Every, K.H. Sutton, P.R. Shewry, A.S. Tatham, T. Coolbear,