Pengembangan Konsep Desain dan Fabrikasi Mesin Penyortir Buah Duku (Lansium Parasiticum)

Pengembangan konsep desain mesin penyortir buah duku (Lansium Parasiticum) dilakukan menggunakan metode Five Step Method. Diperoleh tiga konsep mesin yang kemudian dipilih satu dari tiga konsep terbaik menggunakan metode product champion dilanjutkan dengan pembuatan desain 3D dan Finite Element Analysis (FEA) menggunakan software autodesk inventor 2017. Analisis FEA menunjukkan nilai von Misses stress sebesar 18 MPa bernilai lebih kecil dibanding yield strength material penyusun rangka sebesar 207 MPa, displacement yang terjadi sebesar 0,99 mm dengan nilai safety factor 15. Fabrikasi dan pengujian mesin menunjukkan nilai persentase keberhasilan proses penyortiran pada mesin lebih dari 85% dengan kapasitas sortir 400 kg/jam

WHO/IUIS Allergen Nomenclature: Providing a common language

A systematic nomenclature for allergens originated in the early 1980s, when few protein allergens had been described. A group of scientists led by Dr. David G. Marsh developed a nomenclature based on the Linnaean taxonomy, and further established the World Health Organization/International Union of Immunological Societies (WHO/IUIS) Allergen Nomenclature Sub-Committee in 1986. Its stated aim was to standardize the names given to the antigens (allergens) that caused IgE-mediated allergies in humans. The Sub-Committee first published a revised list of allergen names in 1986, which continued to grow with rare publications until 1994. Between 1994 and 2007 the database was a text table online, then converted to a more readily updated website. The allergen list became the Allergen Nomenclature database (www.allergen.org), which currently includes approximately 880 proteins from a wide variety of sources. The Sub-Committee includes experts on clinical and molecular allergology. They review submissions of allergen candidates, using evidence-based criteria developed by the Sub-Committee. The review process assesses the biochemical analysis and the proof of allergenicity submitted, and aims to assign allergen names prior to publication. The Sub-Committee maintains and revises the database, and addresses continuous challenges as new “omics” technologies provide increasing data about potential new allergens. Most journals publishing information on new allergens require an official allergen name, which involves submission of confidential data to the WHO/IUIS Allergen Nomenclature Sub-Committee, sufficient to demonstrate binding of IgE from allergic subjects to the purified protein

Marker allergens and panallergens in tree and grass pollen allergy

Many allergens from botanically related sources share structural similarities resulting in IgE cross-reactivity. As a consequence, allergens sharing similar structures are often also related on an immunological level, and patients sensitized to one specific allergen may show clinical or in vitro reactivity to structurally similar allergenic proteins of other allergen sources. Different IgE sensitization profiles can be identified in allergic patients according to reactivity to certain allergens. These allergens are defined as marker allergens (Kazemi-Shirazi et al. 2002; Suphioglu 2000; Valenta et al. 2007)

WHO/IUIS Allergen Nomenclature: Providing a common language

Highlights • Beginning and evolution of the official Allergen Nomenclature system 1980–2018. • Allergen Names abbreviated genus, species and number. • Expected data including characterization of protein amino acid sequence, cDNA, human serum donors and experimental data. • Challenges of identifying allergens including exposure and complex human exposure and immunity. • Complexity of new methods including “omics”. Abstract A systematic nomenclature for allergens originated in the early 1980s, when few protein allergens had been described. A group of scientists led by Dr. David G. Marsh developed a nomenclature based on the Linnaean taxonomy, and further established the World Health Organization/International Union of Immunological Societies (WHO/IUIS) Allergen Nomenclature Sub-Committee in 1986. Its stated aim was to standardize the names given to the antigens (allergens) that caused IgE-mediated allergies in humans. The Sub-Committee first published a revised list of allergen names in 1986, which continued to grow with rare publications until 1994. Between 1994 and 2007 the database was a text table online, then converted to a more readily updated website. The allergen list became the Allergen Nomenclature database (www.allergen.org), which currently includes approximately 880 proteins from a wide variety of sources. The Sub-Committee includes experts on clinical and molecular allergology. They review submissions of allergen candidates, using evidence-based criteria developed by the Sub-Committee. The review process assesses the biochemical analysis and the proof of allergenicity submitted, and aims to assign allergen names prior to publication. The Sub-Committee maintains and revises the database, and addresses continuous challenges as new “omics” technologies provide increasing data about potential new allergens. Most journals publishing information on new allergens require an official allergen name, which involves submission of confidential data to the WHO/IUIS Allergen Nomenclature Sub-Committee, sufficient to demonstrate binding of IgE from allergic subjects to the purified protein

Crystal Structures of the Wild Type and the Glu376Gly/Thr255Glu Mutant of Human Medium-Chain Acyl-CoA Dehydrogenase : Influence of the Location of the Catalytic Base on Substrate Specificity

Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active center base-arrangement has been altered to that of long chain acyl-CoA dehydrogenase (LCADH), Glu376Gly/Thr255Glu, have been determined by X-ray crystallography at 2.75 and 2.4 Å resolution, respectively. The catalytic base responsible for the α-proton abstraction from the thioester substrate is Glu376 in MCADH, while that in LCADH is Glu255 (MCADH numbering), located over 100 residues away in its primary amino acid sequence. The structures of the mutant complexed with C8-, C12, and C14-CoA have also been determined. The human enzyme structure is essentially the same as that of the pig enzyme. The structure of the mutant is unchanged upon ligand binding except for the conformations of a few side chains in the active site cavity. The substrate with chain length longer than C12 binds to the enzyme in multiple conformations at its ω-end. Glu255 has two conformations, "active" and "resting" forms, with the latter apparently stabilized by forming a hydrogen bond with Glu99. Both the direction in which Glu255 approaches the Cα atom of the substrate and the distance between the Glu255 carboxylate and the Cα atom are different from those of Glu376; these factors are responsible for the intrinsic differences in the kinetic properties as well as the substrate specificity. Solvent accessible space at the "midsection" of the active site cavity, where the Cα-Cβ bond of the thioester substrate and the isoalloxazine ring of the FAD are located, is larger in the mutant than in the wild type enzyme, implying greater O2 accessibility in the mutant which might account for the higher oxygen reactivity