Thermal aggregation of cod (Gadus morhua) muscle proteins using 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide as a zero length cross-linker.
-
- GILL T. A.
- Canadian Institute of Fisheries Technology, Technical University of Nova Scotia
-
- CONWAY J. T.
- Canadian Institute of Fisheries Technology, Technical University of Nova Scotia
この論文をさがす
抄録
The initial stages of thermally-induced aggregation of cod myofibrils resulted from noncovalent inter molecular cross-linking as demonstrated by SDS electrophoresis. The nature of the noncovalent bonds was studied by introducing a zero length cross-linker, 1-ethyl-3-(3-dimethylamino propyl) carbodiimide (EDC). This allowed the examination of the noncovalent interactions by SDS electrophoresis and quantitative densitometry. Initially, during heating, about 50% of the myosin heavy chain was cross-linked to form a polymerized complex before the involvement of actin, regulatory proteins, or the myosin light chains. Inhibition of thermally-induced noncovalent crosslinking with triglycerides or Triton X-100 as well as the enhancement of aggregation at higher ionic strength, suggested the importance of hydrophobic interaction in this reaction.<br> Cod myosin heavy chains were prepared and the head regions labelled with the fluorescent probe, N-[7(dimethylamino)-4-methyl-3-coumarinyl] maleimide (DACM) which reacts specifically with two thiol groups near the active sites for Ca2+ and EDTA-ATPase. Chymotryptic cleavage of the thermally aggregated myosin heavy chains suggested the involvement of the tail region of the molecule rather than the head in the noncovalent cross-linking reactions.
収録刊行物
-
- Agricultural and Biological Chemistry
-
Agricultural and Biological Chemistry 53 (10), 2553-2562, 1989
公益社団法人 日本農芸化学会
- Tweet
キーワード
詳細情報 詳細情報について
-
- CRID
- 1390282681444951552
-
- NII論文ID
- 110006324024
-
- NII書誌ID
- AA00515312
-
- ISSN
- 18811280
- 00021369
-
- 本文言語コード
- en
-
- データソース種別
-
- JaLC
- Crossref
- CiNii Articles
-
- 抄録ライセンスフラグ
- 使用不可