scholarly journals Clustering ferry ports class-I based on the ferry ro-ro tonnages and main dimensions

2018 ◽  
Vol 181 ◽  
pp. 12001
Author(s):  
Syamsul Asri ◽  
Wahyuddin Mustafa ◽  
Mohammad Rizal Firmansyah ◽  
Farianto Fachruddin Lage
Keyword(s):  
Capacity Constraint ◽  
Class I ◽  
Main Dimension ◽  
Class Ib

Capacity constraint of port for Ferry Port Class I is not clearly stated in the Indonesian National Order of Port Affairs. It only said that ferry ship to be serviced is ships with more than 1000 gross tonnages (GTs). The word more than 1000 GTs is unclear as there are ships with up to 12500 GTs to be serviced in this port. This research introduces cluster of Ferry Port Class I. Ship main dimension and tonnage of sample ships is being used as a basis for the port clustering. The result shows that Ferry Port Class I should be divided into three main Ferry Port Classes I (Class IA, Class IB and Class IC). This new cluster of Ferry Port Class I can be used as a reference in updating the rules regarding ferry port class and as a reference in the design of ferry port main facilities.

scholarly journals A convenient method of preparation of high-activity urease from Canavalia ensiformis by covalent chromatography and an investigation of its thiol groups with 2,2'-dipyridyl disulphide as a thiol titrant and reactivity probe

1976 ◽  
Vol 159 (2) ◽  
pp. 245-257 ◽  
Author(s):  
R Norris ◽  
K Brocklehurst
Keyword(s):  
Convenient Method ◽  
Specific Activity ◽  
Class Ii ◽  
High Reactivity ◽  
Class I ◽  
Thiol Groups ◽  
Class Iii ◽  
Active Centre ◽  
Class Ib ◽  
Covalent Chromatography

1. A convenient method of preparation of jack-bean urease (EC3.5.1.5) involving covalent chromatography by thiol-disulphide interchange is described. 2. Urease thus prepared has specific activity comparable with the highest value yet reported (44.5 ± 1.47 kat/kg, Km = 3.32 ± 0.05 mM; kcat. = 2.15 × 104 ± 0.05 × 104s-1 at pH7.0 and 38°C). 3. Titration of the urease thiol groups with 2,2'-dipyridyl disulphide (2-Py-S-S-2-Py) and application of the method of Tsou Chen-Lu [(1962) Sci. Sin.11, 1535-1558] suggests that the urease molecule (assumed to have mol.wt. 483000 and ε280 = 2.84 × 105 litre·mol-1-cm-1) contains 24 inessential thiol groups of relatively high reactivity (class-I), six ‘essential’ thiol groups of low reactivity (class-II) and 54 buried thiol groups (class-III) which are exposed in 6M-guanidinium chloride. 4. The reaction of the class-I thiol groups with 2-Py-S-S-2-Py was studied in the pH range 6-11 at 25°C(I = 0.1 mol/l) by stopped-flow spectrophotometry, and the analogous reaction of the class-II thiol groups by conventional spectrophotometry. 5. The class-I thiol groups consist of at least two sub-classes whose reactions with 2-Py-S-S-2-Py are characterized by (a) pKa = 9.1, k = 1.56 × 104M-1·s-1 and (b) pKa = 8.1, k = 8.05 × 102M-1·s-1 respectively. The reaction of the class-II thiol groups is characterized by pKa = 9.15 and k = 1.60 × 102M-1·s-1. 6. At pH values 7-8 the class-I thiol groups consist of approx. 50% class-Ia groups and 50% class-Ib groups. The ratio class Ia/class Ib decreases as the pH is raised according to a pKa value ≥ approx. 9.5, and at high pH the class-I thiol groups consist of at most 25% class-Ia groups and at least 75% class-Ib groups. 7. The reactivity of the class-II thiol groups towards 2-Py-S-S-2-Py is insensitive to the nature of the group used to block the class-I thiols. 8. All the ‘essential’ thiol groups in urease appear to be eeactive only as uncomplicated thiolate ions. The implications of this for the active-centre chemistry of urease relative to that of the thiol proteinases are discussed.

scholarly journals In vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules

2006 ◽  
Vol 203 (3) ◽  
pp. 647-659 ◽  
Author(s):  
Jingbo Yan ◽  
Vrajesh V. Parekh ◽  
Yanice Mendez-Fernandez ◽  
Danyvid Olivares-Villagómez ◽  
Srdjan Dragovic ◽  
...  
Keyword(s):  
Cytotoxic T Cells ◽  
Surface Expression ◽  
Proteolytic Processing ◽  
Class I ◽  
Cell Surface Expression ◽  
Peptidase Activity ◽  
Mhc Class Ia ◽  
Class Ib

Endoplasmic reticulum (ER)-associated aminopeptidase (ERAP)1 has been implicated in the final proteolytic processing of peptides presented by major histocompatibility complex (MHC) class I molecules. To evaluate the in vivo role of ERAP1, we have generated ERAP1-deficient mice. Cell surface expression of the class Ia molecules H-2Kb and H-2Db and of the class Ib molecule Qa-2 was significantly reduced in these animals. Although cells from mutant animals exhibited reduced capacity to present several self- and foreign antigens to Kb-, Db-, or Qa-1b–restricted CD8+ cytotoxic T cells, presentation of some antigens was unaffected or significantly enhanced. Consistent with these findings, mice generated defective CD8+ T cell responses against class I–presented antigens. These findings reveal an important in vivo role of ER-associated peptidase activity in tailoring peptides for presentation by MHC class Ia and class Ib molecules.

scholarly journals Function and Regulation of Class I Ribonucleotide Reductase-Encoding Genes in Mycobacteria

2008 ◽  
Vol 191 (3) ◽  
pp. 985-995 ◽  
Author(s):  
Mohube B. Mowa ◽  
Digby F. Warner ◽  
Gilla Kaplan ◽  
Bavesh D. Kana ◽  
Valerie Mizrahi
Keyword(s):  
Mycobacterium Smegmatis ◽  
Chromosomal Region ◽  
Class I ◽  
Growth And Survival ◽  
Ribonucleotide Reductases ◽  
Genes Encoding ◽  
R2 Subunit ◽  
Encoding Genes ◽  
Class Ib

ABSTRACT Ribonucleotide reductases (RNRs) are crucial to all living cells, since they provide deoxyribonucleotides (dNTPs) for DNA synthesis and repair. In Mycobacterium tuberculosis, a class Ib RNR comprising nrdE- and nrdF2-encoded subunits is essential for growth in vitro. Interestingly, the genome of this obligate human pathogen also contains the nrdF1 (Rv1981c) and nrdB (Rv0233) genes, encoding an alternate class Ib RNR small (R2) subunit and a putative class Ic RNR R2 subunit, respectively. However, the role(s) of these subunits in dNTP provision during M. tuberculosis pathogenesis is unknown. In this study, we demonstrate that nrdF1 and nrdB are dispensable for the growth and survival of M. tuberculosis after exposure to various stresses in vitro and, further, that neither gene is required for growth and survival in mice. These observations argue against a specialist role for the alternate R2 subunits under the conditions tested. Through the construction of nrdR-deficient mutants of M. tuberculosis and Mycobacterium smegmatis, we establish that the genes encoding the essential class Ib RNR subunits are specifically regulated by an NrdR-type repressor. Moreover, a strain of M. smegmatis mc2155 lacking the 56-kb chromosomal region, which includes duplicates of nrdHIE and nrdF2, and a mutant retaining only one copy of nrdF2 are shown to be hypersensitive to the class I RNR inhibitor hydroxyurea as a result of depleted levels of the target. Together, our observations identify a potential vulnerability in dNTP provision in mycobacteria and thereby offer a compelling rationale for pursuing the class Ib RNR as a target for drug discovery.

scholarly journals The Class I HLA Repertoire of Pancreatic Islets Comprises the Nonclassical Class Ib Antigen HLA-G

Diabetes ◽  
2006 ◽  
Vol 55 (5) ◽  
pp. 1214-1222 ◽  
Author(s):  
V. Cirulli ◽  
J. Zalatan ◽  
M. McMaster ◽  
R. Prinsen ◽  
D. R. Salomon ◽  
...  
Keyword(s):  
Pancreatic Islets ◽  
Class I ◽  
Class Ib ◽  
Nonclassical Class

scholarly journals Safety Regulations for Alcohol Storage in Laboratories

1999 ◽  
Vol 7 (1) ◽  
pp. 11-11
Author(s):  
Patrick Brooks
Keyword(s):  
Class I ◽  
Laboratory Unit ◽  
Safety Regulations ◽  
Sprinkler Systems ◽  
Flammable Liquids ◽  
Combustible Liquids ◽  
Plastic Containers ◽  
Class Ib ◽  
Combustible Liquid ◽  
Container Capacity

Questions keep arising regarding safety regulations for storage of alcohol and other flammable liquids in a laboratory. I hope what follows sheds some light on this issue.Ethanol is classified as a Class IB combustible liquid, Class IB liquids have a maximum allowable container capacity of 20 liters in “metal (non-DOT approved) or approved plastic containers, safety cans or DOT specification metal drums.”The amount of combustible liquids allowable is determined by the size of the “laboratory unit”. For hospitals with sprinkler systems, per 100 square feet of laboratory space, Class I, II and IIIA (including IB) flammable liquids are limited to 4 L (1.1 gallons) not in approved storage containers or safety cans and 7,5 L (2 gallons) total, including quantities in storage cabinets and safety cans.

scholarly journals Maternal HLA Ib Polymorphisms in Pregnancy Allo-Immunization

2021 ◽  
Vol 12 ◽  
Author(s):  
Gry Persson ◽  
Christophe Picard ◽  
Gregory Marin ◽  
Cecilie Isgaard ◽  
Christina Seefeldt Stæhr ◽  
...  
Keyword(s):  
Human Leukocyte ◽  
Hla Class I ◽  
Maternal Blood ◽  
Class I ◽  
Hla Antibodies ◽  
Leukocyte Antigen ◽  
Primiparous Women ◽  
Class Ib ◽  
In Pregnancy ◽  
Singleton Pregnancies

During pregnancy the formation of alloreactive anti-human leukocyte antigen (HLA) antibodies are a major cause of acute rejection in organ transplantation and of adverse effects in blood transfusion. The purpose of the study was to identify maternal HLA class Ib genetic factors associated with anti-HLA allo-immunization in pregnancy and the degree of tolerance estimated by IgG4 expression. In total, 86 primiparous women with singleton pregnancies were included in the study. Maternal blood samples and umbilical cord samples were collected at delivery. Clinical data were obtained. Maternal blood serum was screened for HLA class I and II antibodies, identification of Donor Specific Antibody (DSA), activation of complement measured by C1q and IgG4 concentrations. Mothers were genotyped for HLA class Ib (HLA-E, -F and -G). Anti-HLA class I and II antibodies were identified in 24% of the women. The maternal HLA-E*01:06 allele was significantly associated with a higher fraction of anti-HLA I immunization (20.0% vs. 4.8%, p = 0.048). The maternal HLA-G 3’-untranslated region UTR4-HLA-G*01:01:01:05 haplotype and the HLA-F*01:03:01 allele were significantly associated with a low anti-HLA I C1q activation (16.7% vs. 57.1%, p = 0.028; 16.7% vs. 50.0%, p = 0.046; respectively). Both HLA‑G and HLA-F*01:03:01 showed significantly higher levels of IgG4 compared with the other haplotypes. The results support an association of certain HLA class Ib alleles with allo-immunization during pregnancy. Further studies are needed to elucidate the roles of HLA-E*01:06, HLA-F*01:03 and HLA‑G UTR4 in reducing the risk for allo-immunization.

scholarly journals Phosphatidylinositol kinases (version 2020.2) in the IUPHAR/BPS Guide to Pharmacology Database

2020 ◽  
Vol 2020 (2) ◽  
Author(s):  
Mohib Uddin
Keyword(s):  
Molecular Weight ◽  
Calcium Binding ◽  
Class Ii ◽  
Catalytic Subunit ◽  
Class I ◽  
Regulatory Subunit ◽  
Class Iii ◽  
Regulatory Subunits ◽  
Phosphatidylinositol 4 ◽  
Class Ib

Phosphatidylinositol may be phosphorylated at either 3- or 4- positions on the inositol ring by PI 3-kinases or PI 4-kinases, respectively.Phosphatidylinositol 3-kinasesPhosphatidylinositol 3-kinases (PI3K, provisional nomenclature) catalyse the introduction of a phosphate into the 3-position of phosphatidylinositol (PI), phosphatidylinositol 4-phosphate (PIP) or phosphatidylinositol 4,5-bisphosphate (PIP2). There is evidence that PI3K can also phosphorylate serine/threonine residues on proteins. In addition to the classes described below, further serine/threonine protein kinases, including ATM (Q13315) and mTOR (P42345), have been described to phosphorylate phosphatidylinositol and have been termed PI3K-related kinases. Structurally, PI3Ks have common motifs of at least one C2, calcium-binding domain and helical domains, alongside structurally-conserved catalytic domains. wortmannin and LY 294002 are widely-used inhibitors of PI3K activities. wortmannin is irreversible and shows modest selectivity between Class I and Class II PI3K, while LY294002 is reversible and selective for Class I compared to Class II PI3K.Class I PI3Ks (EC 2.7.1.153) phosphorylate phosphatidylinositol 4,5-bisphosphate to generate phosphatidylinositol 3,4,5-trisphosphate and are heterodimeric, matching catalytic and regulatory subunits. Class IA PI3Ks include p110α, p110β and p110δ catalytic subunits, with predominantly p85 and p55 regulatory subunits. The single catalytic subunit that forms Class IB PI3K is p110γ. Class IA PI3Ks are more associated with receptor tyrosine kinase pathways, while the Class IB PI3K is linked more with GPCR signalling.Class II PI3Ks (EC 2.7.1.154) phosphorylate phosphatidylinositol to generate phosphatidylinositol 3-phosphate (and possibly phosphatidylinositol 4-phosphate to generate phosphatidylinositol 3,4-bisphosphate). Three monomeric members exist, PI3K-C2α, β and β, and include Ras-binding, Phox homology and two C2domains.The only class III PI3K isoform (EC 2.7.1.137) is a heterodimer formed of a catalytic subunit (VPS34) and regulatory subunit (VPS15).Phosphatidylinositol 4-kinasesPhosphatidylinositol 4-kinases (EC 2.7.1.67) generate phosphatidylinositol 4-phosphate and may be divided into higher molecular weight type III and lower molecular weight type II forms.

scholarly journals The thymus leukemia antigen binds human and mouse CD8.

1991 ◽  
Vol 174 (5) ◽  
pp. 1131-1138 ◽  
Author(s):  
M Teitell ◽  
M F Mescher ◽  
C A Olson ◽  
D R Littman ◽  
M Kronenberg
Keyword(s):  
Binding Site ◽  
Class I ◽  
Antigen Binding ◽  
Gamma Delta ◽  
Antigen Binding Site ◽  
Peptide Antigen ◽  
Transplantation Antigens ◽  
Human And Mouse ◽  
Class Ib ◽  
Leukemia Antigen

The thymus leukemia antigen (TLA) is a class Ib, or 'nonclassical' class I molecule, one of several encoded within the Tla locus of the mouse major histocompatibility complex (MHC). It structurally resembles the H-2K, D, and L class I transplantation antigens, which present processed peptides to cytotoxic T lymphocytes (CTLs). Although their function(s) are unknown, there has been recent speculation concerning the possibility that class Ib molecules may present antigens to T cells that express gamma delta T cell antigen receptors (TCRs). In this report, using both a cell-cell adhesion assay and adhesion of T lymphocyte clones to purified plate-bound TLA, we provide evidence that TLA can bind to both human and mouse CD8. We also show that a chimeric class I molecule containing the peptide antigen binding site of Ld and the alpha 3 domain, transmembrane, and cytoplasmic segments of TLA, can support a CD8-dependent immune response by CTLs. These results demonstrate for the first time binding of a class Ib molecule to CD8 with a functional outcome, as is observed for the class I transplantation antigens. The capacity to interact with CD8 has been conserved despite the extensive sequence divergence of TLA in the peptide antigen binding site, suggesting this interaction is highly significant. TLA is expressed by epithelial cells in the mouse small intestine. As these epithelial cells are in close contact with intestinal intraepithelial lymphocytes that are nearly all CD8+, and many of which express the gamma delta TCR, the data are consistent with the hypothesis that TLA is involved in antigen presentation, perhaps to gamma delta-positive lymphocytes in this site.

scholarly journals Class I dependence of the development of CD4+ CD8- NK1.1+ thymocytes.

1994 ◽  
Vol 180 (1) ◽  
pp. 395-399 ◽  
Author(s):  
M C Coles ◽  
D H Raulet
Keyword(s):  
T Cells ◽  
Class Ii ◽  
Class I ◽  
Thymic Epithelial Cells ◽  
Small Subset ◽  
Class I Mhc ◽  
Histocompatibility Complex ◽  
Deficient Mice ◽  
Class Ib ◽  
Selection Of

A small subset of functionally active CD4+ CD8- thymocytes express the NK1.1 marker, as do most CD4-CD8- NK1.1+ thymocytes. Previous studies have failed to implicate a role for major histocompatibility complex (MHC) or related molecules in the selection of the CD4+ CD8- NK1.1+ subset. We report here that the development of most of these cells is sharply reduced in class I-deficient mice, but not in class II-deficient mice. Hence, some CD4+ T cells are class I dependent and not class II dependent. Unlike conventional T cells, however, the development of NK1.1+ thymocytes in both the CD4+ CD8- and CD4- CD8- subsets is dependent on class I MHC expression by hematopoietic cells and not thymic epithelial cells. We propose that these populations are selected by nonpolymorphic class Ib or CD1 molecules.

scholarly journals Phosphatidylinositol kinases in GtoPdb v.2021.3

2021 ◽  
Vol 2021 (3) ◽  
Author(s):  
Mohib Uddin
Keyword(s):  
Molecular Weight ◽  
Calcium Binding ◽  
Class Ii ◽  
Catalytic Subunit ◽  
Class I ◽  
Regulatory Subunit ◽  
Class Iii ◽  
Regulatory Subunits ◽  
Phosphatidylinositol 4 ◽  
Class Ib

Phosphatidylinositol may be phosphorylated at either 3- or 4- positions on the inositol ring by PI 3-kinases or PI 4-kinases, respectively.Phosphatidylinositol 3-kinasesPhosphatidylinositol 3-kinases (PI3K, provisional nomenclature) catalyse the introduction of a phosphate into the 3-position of phosphatidylinositol (PI), phosphatidylinositol 4-phosphate (PIP) or phosphatidylinositol 4,5-bisphosphate (PIP2). There is evidence that PI3K can also phosphorylate serine/threonine residues on proteins. In addition to the classes described below, further serine/threonine protein kinases, including ATM (Q13315) and mTOR (P42345), have been described to phosphorylate phosphatidylinositol and have been termed PI3K-related kinases. Structurally, PI3Ks have common motifs of at least one C2, calcium-binding domain and helical domains, alongside structurally-conserved catalytic domains. wortmannin and LY 294002 are widely-used inhibitors of PI3K activities. wortmannin is irreversible and shows modest selectivity between Class I and Class II PI3K, while LY294002 is reversible and selective for Class I compared to Class II PI3K.Class I PI3Ks (EC 2.7.1.153) phosphorylate phosphatidylinositol 4,5-bisphosphate to generate phosphatidylinositol 3,4,5-trisphosphate and are heterodimeric, matching catalytic and regulatory subunits. Class IA PI3Ks include p110α, p110β and p110δ catalytic subunits, with predominantly p85 and p55 regulatory subunits. The single catalytic subunit that forms Class IB PI3K is p110γ. Class IA PI3Ks are more associated with receptor tyrosine kinase pathways, while the Class IB PI3K is linked more with GPCR signalling.Class II PI3Ks (EC 2.7.1.154) phosphorylate phosphatidylinositol to generate phosphatidylinositol 3-phosphate (and possibly phosphatidylinositol 4-phosphate to generate phosphatidylinositol 3,4-bisphosphate). Three monomeric members exist, PI3K-C2α, β and β, and include Ras-binding, Phox homology and two C2 domains.The only class III PI3K isoform (EC 2.7.1.137) is a heterodimer formed of a catalytic subunit (VPS34) and regulatory subunit (VPS15).Phosphatidylinositol 4-kinasesPhosphatidylinositol 4-kinases (EC 2.7.1.67) generate phosphatidylinositol 4-phosphate and may be divided into higher molecular weight type III and lower molecular weight type II forms.

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