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At least 127 records · Page 7Linked to original sources
PubMed1995

Enhancing effects of chicken egg white derivatives on the phagocytic response in the dog.

Immunostimulative effects of chicken egg white derivatives (EWD) on phagocytic responses of peripheral blood mononuclear cells (MNC) and polymorphonuclear cells (PMN) in dogs were evaluated by flow cytometric analysis. Peripheral blood leukocytes (PBL) cultured with EWD showed the enhanced phagocytic response. The response was maximal when PBL were cultured with 100 - 400 micrograms/ml of EWD for 3 - 12 hr. Furthermore, significantly increased phagocytic responses were also induced even when PBL were cultured with protein components (200 micrograms/ml) of EWD such as conalbumin, flavoprotein and ficin-papain inhibitor for 3 hr. In addition, the enhancing effect of EWD on the phagocytic responses was also observed in MNC cultured with EWD (200 micrograms/ml) for 4 hr but not in PMN cultured with EWD in the same procedures. The supplement of the supernatant (20%) of MNC cultured with EWD (200 micrograms/ml) for 24 hr at 37 degrees C to PBL and MNC resulted in the enhancement of their phagocytic responses. In contrast, the supernatant of PMN cultured with EWD for 24 hr at 37 degrees C did not show any significant enhancing effect on the phagocytic responses of PBL, MNC and PMN. These results suggest that EWD has an enhancing effect on phagocytosis of MNC and PMN, which may be mediated through active humoral substances produced by EWD-stimulated MNC.

Adjuvants, Immunologic↗
PubMed1984

Rh0(D) activity of red blood cells and stroma treated with proteolytic enzymes.

Agglutinability of red blood cells against anti-D increased remarkably when the cells were treated with proteolytic enzymes, such as bromelain, chymotrypsin, ficin, papain, pronase and trypsin. When stroma prepared from normal red blood cells was treated with any of proteolytic enzymes, however, Rh-Hr blood type activities were completely abolished. The similar results were obtained from stroma solubilized with detergents which was treated with enzymes after being prepared. Of all the enzymes, ficin acted more slowly than the others did. Neuraminidase or phospholipase A2 had no effect on Rh-Hr activities at all. SDS-polyacrylamide gel electrophoretic pattern of stroma prepared from bromelain, ficin and pronase-treated red blood cells were quite different from that of normal stroma.

Bromelains↗
PubMed1991

Comparison of in vitro techniques to the in situ technique for estimation of ruminal degradation of protein.

The accuracy with which the Streptomyces griseus, ficin, and neutral protease with amylase in vitro methods could be used to predict in situ protein degradation of concentrate feeds was evaluated. Four types of soy products and two types of distillers grains were incubated using each of the four techniques for .5, 1, 2, 4, 8, 12, 24, and 48 h. The percentages of initial CP that remained undegraded over time were determined. Comparison of the degradation curves and contrast analysis of the data indicated that the in vitro methods generated degradability estimates in conflict with those obtained by the in situ method. However, the neutral protease with amylase method ranked the test feeds according to the extent of CP degradation at 24 h most similar to that in situ. Regression equations developed with the neutral protease with amylase degradability estimates explained 78, 76, and 74% of the variation in the in situ estimates obtained after 12, 18, and 24 h of incubation, respectively. At least 69% of the variation in the 18-h in situ estimates could be explained by the neutral protease with amylase estimates obtained after 1, 2, 4, 8, and 12 h of incubation. Little relationship was found between the ficin and S. griseus versus in situ results. Although none of the in vitro methods resulted in degradation curves consistently related to those generated by the in situ technique, relationships were found between protein degradability estimates obtained by the neutral protease with amylase method at specific time points and those obtained by the in situ technique.

Amylases↗
PubMed1997

Protein degradation in response to spontaneous heating in alfalfa hay by in situ and ficin methods.

Alfalfa forage, field-wilted to 29.9 or 19.7% moisture and packaged in five baling treatments (prestorage control; conventional bales; and laboratory bales made at 1.0, 1.5, and 2.0 times the density of conventional bales), was evaluated for protein degradation characteristics by in situ and ficin assays. Relationships between degradation rates and accumulated heating degree days suggested that these degradation rates are controlled by two conditions. Degradation rates increased concurrently with conservation and minimal heating, primarily because of a large redistribution of highly degradable N that was soluble in prestorage controls, but not in conserved hays. For both methods, this effect appeared to be maximized between 100 and 125 heating degree days. With respect to the in situ method, these effects appeared to be less pronounced, and degradabilities were not affected. After bales accumulated about 125 heating degree days, degradation rates decreased predictably in response to heating by both methods, as did N degradabilities calculated from in situ data. Increases in degradation rates concurrent with conservation and minimal heating appear to be especially important considerations when results of the ficin assay are being interpreted.

Analysis of Variance↗
PubMed1976

Purification and properties of two protease inhibitors from rat skin inhibiting papain and other SH-proteases.

Two papain inhibitors, I1 and I2, from rat skin extract were purified by affinity chromatography on KSCN-modified papain-agarose gel and by gel filtration on Sephadex G-100. I1 had a molecular weight of 74 000, a pI of 4.6, and it contained 4% of carbohydrates. I1 inhibited papain, ficin, bromelain, rat skin benzoylarginine-2-naphthylamide hydrolase, and to a minor extent, rat skin cathepsin C and bovine trypsin. Bovine chymotrypsin or rat skin cathepsin D were not inhibited and benzoylarginine-2-naphthylamide hydrolase was inhibited only at alkaline pH. An inhibitor corresponding to I1 was present in various rat tissues and also in serum. A similar inhibitor was present in the skin of cat, rabbit, guinea pig, and man. I2 had a molecular weight of 13 400, a pI of 4.9 and it contained no carbohydrates. I2 inhibited all thiol proteases tested, but not trypsin, chymotrypsin, or rat skin cathepsin D. I2 formed an equimolar complex with papain and benzoylarginine-2-naphthylamide hydrolase. I2 was present in rat skin, muscle, lung, and small intestine, but not in kidney, liver, or serum. A similar inhibitor was found in skin extracts of cat, rabbit, guinea pig, and man.

Animals↗
PubMed2002

A fully recombinant partial prothrombin complex effectively bypasses fVIII in vitro and in vivo.

The development of inhibitory antibodies is a serious complication in hemophilic patients, severely compromising therapeutic success. Bleeding episodes in affected patients are controlled by treatment with a plasma-derived prothrombin complex concentrate (PCC), activated PCC (APCC) or recombinant activated factor VII. We hypothesized that a recombinant two-component agent consisting of recombinant prothrombin (rfII) and activated factor X (rfXa) would have substantial fVIII bypassing activity and could be a safe alternative therapeutic option. To test this hypothesis we assembled an agent in vitro solely consisting of rfII and rfXa at a molar ratio of 37,500:1. These factors are believed to be responsible for the activity of APCC preparations. Recombinant fX, used as the source for fXa generation, and rfII were purified from serum-free and protein-free conditioned media of stably transfected CHO and BHK tissue culture cells, respectively. Activation of rfX to rfXa was accomplished by the plant protease ficin, obviating the need for a protease derived from a human or animal source. We found that in vitro the complex reduced the abnormally prolonged activated partial thromboplastin time (APTT) of a high-titer fVIII inhibitor plasma similar to an APCC preparation. Furthermore, addition of increasing amounts of rfII/rfXa to inhibitor plasma resulted in a linear dose-dependent increase in the rate of thrombin generation. In a rabbit fVIII inhibitor model, treatment with rfII/rfXa statistically significantly reduced the intensity of the abnormal cuticle bleeding. In the Wessler test, rfII/rfXa showed no thrombogenicity. These data show that a well-defined, particularly safe and efficacious agent with fVIII bypassing activity can be generated from recombinant fII and fXa.

Animals↗