Topic
Proteolytic enzymes
About: Proteolytic enzymes is a research topic. Over the lifetime, 23096 publications have been published within this topic receiving 835544 citations.
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TL;DR: Low-molecular-mass beta-(2,6)-linked fructose-oligosaccharides were examined as a new carbohydrate source for growth of bifidobacteria and showed the best growth, produced the highest amounts of organic acids and metabolized both short- and long-chain beta-FOS.
Abstract: Low-molecular-mass beta-(2,6)-linked fructose-oligosaccharides (beta-(2,6)-FOS) were examined as a new carbohydrate source for growth of bifidobacteria. beta-(2,6)-FOS were prepared from microbial high-molecular-mass levan by acid hydrolysis and refined by cation-exchange chromatography. (13)C-NMR spectroscopy confirmed the presence of predominantly beta-(2,6)-fructosyl linkages in the oligosaccharides. More than 80% beta-(2,6)-FOS was recovered after in vitro incubation with amylolytic and proteolytic enzymes, implying resistance to degradation in the upper intestinal tract. Bifidobacterium adolescentis, B. longum, B. breve, and B. pseudocatenulatum were studied in vitro for their ability to metabolize beta-(2,6)-FOS. Growth, decrease in pH, formation of short- chain fatty acids (lactate, acetate, formate) and degradation of beta-(2,6)-FOS were markedly different among species. B. adolescentis showed the best growth, produced the highest amounts of organic acids and metabolized both short- and long-chain beta-(2, 6)-FOS.
163 citations
TL;DR: This work reports that, in Chlamydomonas reinhardtii, the cDNA-cloned sequence of a GPX homologue contains an internal TGA codon in frame to the ATG, the first direct proof that a UGA opal codon is decoded in the plant kingdom to incorporate selenocysteine.
163 citations
TL;DR: In this paper, a mathematical model of cancer cell invasion of tissue (extracellular matrix) is proposed, which consists of a system of reaction-diffusion-taxis partial differential equations, with nonlocal (integral) terms describing the interactions between cancer cells and the host tissue.
Abstract: In this paper we consider a mathematical model of cancer cell invasion of tissue (extracellular matrix). Two crucial components of tissue invasion are (i) cancer cell proliferation, and (ii) over-expression and secretion of proteolytic enzymes by the cancer cells. The proteolytic enzymes are responsible for the degradation of the tissue, enabling the proliferating cancer cells to actively invade and migrate into the degraded tissue. Our model focuses on the role of nonlocal kinetic terms modelling competition for space and degradation. The model consists of a system of reaction-diffusion-taxis partial differential equations, with nonlocal (integral) terms describing the interactions between cancer cells and the host tissue. First of all we prove results concerning the local existence, uniqueness and regularity of solutions. We then prove global existence. Using Green's functions, we transform our original nonlocal equations into a coupled system of parabolic and elliptic equations and we undertake a numerical analysis of this equivalent system, presenting computational simulation results from our model showing the effect of the nonlocal terms (travelling waves we observed have the shape closely linked to the nonlocal terms). Finally, in the discussion section, concluding remarks are made and open problems are indicated.
163 citations
TL;DR: The structure and composition of protein bodies, and the role of enzymes in this structure and structure change, have been investigated in more detail in this chapter.
Abstract: INTRODUCTION 95 PROTEIN BODIES ........ ...... ... ..... ... ....... .. ... ... ..... ... ... .... . . .. 96 Protein Body Distribution ........ 96 Protein Body Structure and Composition . .. . . .. . . . ... ... . .. . ....... . ... ... . . .. ... . .. ... .. ... ... ... ... ... 97 Protein Body Fate ....... ... ... . . . .... .... ... ... . ... 98 Internal degradation and fusion ....... ...... .... ... . ..... ..... 98 Peripheral degradation and fusion ...... . . . . . . . . . . . . . . . . . . . . . . 100 Subunit degradation 100 STORAGE PROTEINS OF SEEDS ... ...... ...... 101 PROTEOLYTIC ENZYMES ....... ..... 103 Endopeptidases . . ... ..... ... ... ... . ....... ........ . .. 103 Properties of endopeptidases . 104 Localization of endopeptidases . . . . . . ....... ......... ...... .... . . . . . .. . 105 E;r;opeptidases 108 Aminopeptidases . . . . . 108 Carboxypeptidases . . . . . . . . . . . . . . . . :..... 110 Dipeptidases 110 Control 0/ Proteolytic Enzymes 110 CONCLUDING REMARKS . .. ... ... ...... 114
163 citations
TL;DR: The aim of this review is to summarize some of the characteristics of the aspartic protease family, a group of proteolytic enzymes that share the same catalytic apparatus.
Abstract: The Aspartic proteases (EC 3.4.23) are a group of proteolytic enzymes that share the same catalytic apparatus. Members of the aspartic protease family can be found in different organisms, ranging from humans to plants and retroviruses. The best known sources of aspartic proteases are the stomach of mammals, yeast and fungi, with porcine pepsin as the proto type. The aim of this review is to summarize some of the characteristics of the aspartic protease family.
163 citations