Quinta pars huius operis in se contine[n]s glosam ordinariam cu[m] expositio[n]e lyre litterali [et] morali : necnon additionibus ac replicis : super libros, Matthei, Marci, Luce, Ioha[n]nis.

Pie de imp. tomado del colofón de la sexta parte

Quinta pars huius operis in se contine[n]s glosam ordinariam cu[m] expositio[n]e lyre litterali [et] morali : necnon additionibus ac replicis : super libros, Matthei, Marci, Luce, Ioha[n]nis.

Pie de imp. tomado del colofón de la sexta parte

Sexta pars biblie cu[m] glosa ordinaria [et] expositio[n]e lyre litterali [et] morali : necno[n] additio[n]ib[us] ac replicis : sup[er] Ep[istol]as ad Romanos, Corinthios, Galathas, Ephesios, Philippenses, Colossenses, Thessalonicenses, Timotheum, Titum,

Capitulares miniadas

Sacrae ecclesiae orationes : (quas vulgo collectas vocamus) & hybernae & aestiuae partiu[m] ta[m] de tempore q[uam] de sanctis, cu[m] no[n]nullis conclusionu[m] regulis, ex probatissimis diuinor[um] officiorum codicibus atte[n]tis no[n] minus orthographia

Capitulares grab. xil.

Quinta pars huius operis co[n]tine[n]s postillam / d[omi]ni Hugonis Cardinalis super quattuor eua[n]gelia s[e]c[un]d[u]m Mattheu[m], Marcum, Lucam, Iohannem.

Sign.: a8, b6, c8, d6, e8, f6, g8, h6, i8, k6, l8, m6, n8, o6, p8, q6, r8, s6, t8, u6, x8, y6, z8, A6, B8, C6, D8, E6, F8, G6, H8, I6, K8, L6, M8, N6, O8, P6, Q8, R6, S8, T6, U8, X6, Y8, Z6, 2A8, 2B6, 2C8, 2D-2F6

Margarita poetica

Descripción basada en: Tomado de Craviotto I, 2370

Historiae romanae decades.

Marca tip. en colofón

El espíritu de Maquiavelo, esto es, reflexiones de D. Antonio Eximeno sobre el elogio de Nicolás Maquiavelo, dicho en la Academia Florentina por el Sr. Juan Bautista Baldelli en el año 1794

Índice

Sermones quadragesimales [Texto impreso]

Colofón

Gulielmi Rondeletii... Libri de Piscibus Marinis. [Texto impreso]

Marca tip. en port

Ramilletillo de las Divinas Flores [Texto impreso] : escogidas del delicioso jardin de la Iglesia ...

Sign.: A-G8, H6

A Double-Strand Break Repair Component Is Essential for S Phase Completion in Fission Yeast Cell Cycling

Fission yeast rad22+, a homologue of budding yeast RAD52, encodes a double-strand break repair component, which is dispensable for proliferation. We, however, have recently obtained a cell division cycle mutant with a temperature-sensitive allele of rad22+, designated rad22-H6, which resulted from a point mutation in the conserved coding sequence leading to one amino acid alteration. We have subsequently isolated rad22+ and its novel homologue rti1+ as multicopy suppressors of this mutant. rti1+ suppresses all the defects of cells lacking rad22+. Mating type switch-inactive heterothallic cells lacking either rad22+ or rti1+ are viable, but those lacking both genes are inviable and arrest proliferation with a cell division cycle phenotype. At the nonpermissive temperature, a synchronous culture of rad22-H6 cells performs DNA synthesis without delay and arrests with chromosomes seemingly intact and replication completed and with a high level of tyrosine-phosphorylated Cdc2. However, rad22-H6 cells show a typical S phase arrest phenotype if combined with the rad1-1 checkpoint mutation. rad22+ genetically interacts with rad11+, which encodes the large subunit of replication protein A. Deletion of rad22+/rti1+ or the presence of rad22-H6 mutation decreases the restriction temperature of rad11-A1 cells by 4–6°C and leads to cell cycle arrest with chromosomes incompletely replicated. Thus, in fission yeast a double-strand break repair component is required for a certain step of chromosome replication unlinked to repair, partly via interacting with replication protein A.

A strategy for the identification of proteins targeted by thioredoxin

Thioredoxins are 12-kDa proteins functional in the regulation of cellular processes throughout the animal, plant, and microbial kingdoms. Growing evidence with seeds suggests that an h-type of thioredoxin, reduced by NADPH via NADP-thioredoxin reductase, reduces disulfide bonds of target proteins and thereby acts as a wakeup call in germination. A better understanding of the role of thioredoxin in seeds as well as other systems could be achieved if more were known about the target proteins. To this end, we have devised a strategy for the comprehensive identification of proteins targeted by thioredoxin. Tissue extracts incubated with reduced thioredoxin are treated with a fluorescent probe (monobromobimane) to label sulfhydryl groups. The newly labeled proteins are isolated by conventional two-dimensional electrophoresis: (i) nonreducing/reducing or (ii) isoelectric focusing/reducing SDS/PAGE. The isolated proteins are identified by amino acid sequencing. Each electrophoresis system offers an advantage: the first method reveals the specificity of thioredoxin in the reduction of intramolecular vs. intermolecular disulfide bonds, whereas the second method improves the separation of the labeled proteins. By application of both methods to peanut seed extracts, we isolated at least 20 thioredoxin targets and identified 5—three allergens (Ara h2, Ara h3, and Ara h6) and two proteins not known to occur in peanut (desiccation-related and seed maturation protein). These findings open the door to the identification of proteins targeted by thioredoxin in a wide range of systems, thereby enhancing our understanding of its function and extending its technological and medical applications.