Alteration of Intestinal Microbiome of Infected Hamsters during the Treatment with Specific Cow Antibodies.

infection (CDI) often develops after pretreatment with antibiotics, which can lead to damage of the intestinal microbiome. The approach of this study was to use specific polyclonal antibodies isolated from the milk of immunized cows to treat CDI, in contrast to the standard application of nonspecific antibiotics. To gain a deeper understanding of the role of the microbiome in the treatment of CDI with bovine antibodies, stool and intestinal fluid samples of hamsters were collected in large quantities from various treatments (>400 samples).

Data concerning the fractionation of individual whey proteins and casein micelles by microfiltration with ceramic gradient membranes.

Data are related to the research article "Fractionation of casein micelles and immunoglobulins by microfiltration in diafiltration mode Study of the transmission and yield of IgG, IgA and IgM" [1]. The data show the transmission and yield of the individual whey proteins α-Lactalbumin (α-La), β -Lactoglobulin (β -Lg), blood serum albumin (BSA), lactoferrin (LF), lactoperoxidase (LPO) and the immunoglobulins IgG, IgA, IgM during microfiltration (0.14 μm) performed in diafiltration mode at 50 °C with different applied transmembrane pressures (0.

Technical Concepts for the Investigation of Spatial Effects in Spiral-Wound Microfiltration Membranes.

Existing works on the influence of spatial effects on flux and permeation of proteins in microfiltration (MF) have focused on ceramic membranes. There is little information on spiral-wound membranes (SWMs). Since the inner core of a SWM is practically inaccessible by non-destructive techniques, three different prototypes were constructed in this study to optimize suitability for the investigation of spatial effects on filtration performance.

Milk Protein Fractionation by Means of Spiral-Wound Microfiltration Membranes: Effect of the Pressure Adjustment Mode and Temperature on Flux and Protein Permeation.

Protein fractionation by means of microfiltration (MF) is significantly affected by fouling, especially when spiral-wound membranes (SWMs) are used. We investigated the influence of the mode of transmembrane pressure (Δp) increase to target level and the deposit layer pressure history on the filtration performance during skim milk MF at temperatures of 10 °C and 50 °C. Two filtration protocols were established: No.

Treatment and Prevention of Recurrent Clostridium difficile Infection with Functionalized Bovine Antibody-Enriched Whey in a Hamster Primary Infection Model.

Toxin-induced infection (CDI) is a major disease characterized by severe diarrhea and high morbidity rates. The aim with this study was to develop an alternative drug for the treatment of CDI. Cows were repeatedly immunized to establish specific immunoglobulin G and A titers against toxins A (TcdA) and B (TcdB) and against cells in mature milk or colostrum.

Data concerning the chromatographic isolation of bovine IgG from milk- and colostral whey.

Data included are related to the research article "Isolation of biofunctional bovine immunoglobulin G from milk- and colostral whey with mixed-mode chromatography at lab and pilot scale" (Heidebrecht et al., 2018) [1]. Data show individual bovine whey proteins in flow-through and elution fractions using different chromatographic resins as well as different binding and elution conditions.

Concentration of Immunoglobulins in Microfiltration Permeates of Skim Milk: Impact of Transmembrane Pressure and Temperature on the IgG Transmission Using Different Ceramic Membrane Types and Pore Sizes.

The use of bioactive bovine milk immunoglobulins (Ig) has been found to be an alternative treatment for certain human gastrointestinal diseases. Some methodologies have been developed with bovine colostrum. These are considered in laboratory scale and are bound to high cost and limited availability of the raw material.

Isolation of biofunctional bovine immunoglobulin G from milk- and colostral whey with mixed-mode chromatography at lab and pilot scale.

The aim of the present work was to develop a new scalable and cost-efficient process to isolate bovine immunoglobulin G from colostral whey with high purity and minimal loss of activity. The mixed mode material Mercapto-Ethyl-Pyridine-Hypercel™ was identified appropriate for direct capture of immunoglobulin G. The binding mechanism is primarily based on hydrophobic interactions at physiological conditions.

Lysyl oxidase like-4 monoclonal antibody demonstrates therapeutic effect against head and neck squamous cell carcinoma cells and xenografts.

A new member of the lysyl oxidase (LOX) family, lysyl oxidase-like 4 (LOXL4), is overexpressed in head and neck squamous cell carcinoma (HNSCC) compared to normal squamous epithelium. A monoclonal antibody (mAb) derived from fusion of Balb/c mouse splenocytes immunized with LOXL4 specific peptide was used to evaluate its therapeutic efficacy in 15 HNSCC cell lines associated with LOXL4 overexpression. For xenograft experiments 41 severe combined immunodeficient (SCID) mice were used to analyze LOXL4-mAb mediated tumor regression.

Down-regulation of the cancer/testis antigen 45 (CT45) is associated with altered tumor cell morphology, adhesion and migration.

Background: Due to their restricted expression in male germ cells and certain tumors, cancer/testis (CT) antigens are regarded as promising targets for tumor therapy. CT45 is a recently identified nuclear CT antigen that was associated with a severe disease score in Hodgkin's lymphoma and poor prognosis in multiple myeloma. As for many CT antigens, the biological function of CT45 in developing germ cells and in tumor cells is largely unknown.

Regulation of repp86 stability by human Siah2.

Human repp86 is a nuclear protein that is expressed in a tightly limited period of time during the cell cycle and plays an essential role in its progression. Manipulation of repp86 expression by reduction of endogenous repp86 or overexpression of exogenous repp86 results in cell cycle arrest. We found that repp86 interacts with human Siah2, which is a known mediator for proteasomal degradation.

Characterization and expression of CT45 in Hodgkin's lymphoma.

Purpose: The monoclonal antibody Ki-A10 (IgG1) generated after immunization of mice with Hodgkin's lymphoma cell line L428 detects a nuclear antigen in human tissues with a restricted distribution pattern similar to cancer/testis antigens. The aim of this study was to characterize the antigen and to determine the expression profile in Hodgkin's lymphoma.

Experimental Design: The half-life and phosphorylation of the antigen were determined by radiolabeling.

Human EML4, a novel member of the EMAP family, is essential for microtubule formation.

Human EML4 (EMAP-like protein 4) is a novel microtubule-associated WD-repeat protein of 120 kDa molecular weight, which is classified as belonging to the conserved family of EMAP-like proteins. Cosedimentation assays demonstrated that EML4 associates with in vitro polymerized microtubules. Correspondingly, immunofluorescence stainings and transient expression of EGFP-labeled EML4 revealed a complete colocalization of EML4 with the interphase microtubule array of HeLa cells.

Repp86 expression and outcome in patients with neuroblastoma.

Purpose: Given the well-known challenges of neuroblastoma prognosis, we investigated whether the expression of restrictedly expressed proliferation-associated protein of 86 kDa theoretical molecular mass (repp86), a proliferation-associated protein expressed in S, G2, and M phases of the cell cycle, correlates with the clinical outcome in patients with neuroblastoma.

Patients And Methods: 161 children with different stages of neuroblastoma were studied; the median follow-up time was 72.8 months.

repp86: A human protein associated in the progression of mitosis.

Human repp86 becomes detectable in the nucleoplasm of cycling cells at the G(1)-S boundary, condenses at the centrosomes with the onset of mitosis, during which it progressively locates to the mitotic spindle and to the midbody, and vanishes at the completion of cytokinesis. The repp86 cDNA was cloned and sequenced. Full-length repp86 and its COOH-terminal domain cosediment with polymerized microtubules, linking repp86 to the family of microtubule-associated proteins.

Concurrent overexpression of p53 and c-erbB-2 correlates with accelerated cycling and concomitant poor prognosis in node-negative breast cancer.

Simultaneous overexpression of c-erbB-2 and p53 has been reported to be prognostically unfavorable in breast cancer. Herein, we show that concurrent overexpression of these 2 proteins is associated with a marked reduction in the relative fraction of cells in G(1) phase of the cell cycle, indicating an accelerated cell cycle progression. Using an immunohistochemical approach, we examined 261 cases of node-negative infiltrating ductal carcinomas of the breast with respect to c-erbB-2 and p53 expression and to the proliferative activity measured by the Ki-67 index.

Cloning and localization of C2orf2(ropp120), a previously unknown WD repeat protein.

Ropp 120 (restrictedly overexpressed proliferation-associated protein) is a cytoplasmic protein of 120 kDa that is significantly overexpressed in mitotic cells. Protein sequencing of the immunoaffinity purified 120-kDa protein showed it to be an as yet unknown protein. DNA sequencing revealed a cDNA sequence of 3419 bases, which includes the complete coding region of ropp120 of 2943 bases (981 amino acids).

Immunoenzymatic detection of the new proliferation associated protein p100 by means of a cellular ELISA: specific detection of cells in cell cycle phases S, G2 and M.

In vitro proliferation assays are widely used in biomedical research. We describe the immunoenzymatic (ELISA) detection of a recently described proliferation associated protein (p100) by means of a new monoclonal mouse IgG1 antibody (Ki-S2). P100 is a 100 kDa nuclear protein that is specifically detected during the cell cycle phases S, G2 and M.

Immunologic proliferation marker Ki-S2 as prognostic indicator for lymph node-negative breast cancer.

Background: Proper treatment of lymph node-negative breast cancer depends on an accurate prognosis. To improve prognostic models for this disease, we evaluated whether an immunohistochemical marker for proliferating cells, Ki-S2 (a monoclonal antibody that binds to a 100-kd nuclear protein expressed in S, G2, and M phases of the cell cycle), is an accurate indicator of prognosis.

Methods: We studied 371 Swedish women with lymph node-negative breast cancer; the median follow-up time was 95 months.

The immunohistochemical marker Ki-S2: cell cycle kinetics and tissue distribution of a novel proliferation-specific antigen.

The monoclonal antibody Ki-S2 binds to a recently characterized proliferation-specific protein, p100. To assess its distribution pattern under physiologic and pathologic conditions, we performed immunohistochemical analyses on an exhaustive spectrum of normal tissues, 624 miscellaneous solid cancers, and 95 hematologic malignancies, and compared the results with Ki-67 immunostaining on consecutive sections. In addition, Ki-S2 expression was related to the DNA content by dual parameter flow cytometric analysis in parallel with Ki-67 labeling using a human cancer cell line.

Sinus-lining cells of the lymph nodes recognized as a dendritic cell type by the new monoclonal antibody Ki-M9.

In the immunobiological characterization of lymph node cells, sinus-lining cells (SLCs) have been given little attention mainly due to the difficulties in their recognition. Ki-M9 is a new monoclonal antibody (MAb) selected for its unique capability to visualize SLCs in human lymph nodes. The details were established by light and electron microscopy and immunoprecipitation of the corresponding biosynthetically labeled antigen.

p100: a novel proliferation-associated nuclear protein specifically restricted to cell cycle phases S, G2, and M.

By immunization with nuclear lysates of L428 cells, we raised a monoclonal mouse antibody, Ki-S2 (IgG1). In Western blots, this antibody recognizes a nuclear antigen with an apparent molecular mass of 100 kD, termed p100. Protein sequencing of p100 showed that this is a hitherto unknown protein.

Detection of human topoisomerase II alpha in cell lines and tissues: characterization of five novel monoclonal antibodies.

We report five novel monoclonal antibodies (Ki-S1, Ki-S4, Ki-S6, Ki-S7, and Ki-S8) reactive with a proliferation-related nuclear antigen. In immunoprecipitation and Western blot experiments using crude nuclear extracts, they recognized a protein of 170 kD that, after proteolytic digestion of the immunoprecipitate and sequencing of the resulting peptides, was identified as the alpha-isoform of human topoisomerase II. This was confirmed by testing the antibodies on a highly purified enzyme preparation.