Low prevalence of positive interferon-gamma tests in HIV-positive long-term immigrants in Norway.

OBJECTIVE: To determine the prevalence and predictors of positive interferon-gamma release assays (IGRAs) and tuberculin skin tests (TSTs) in human immunodeficiency virus (HIV) infected patients in Norway, a low tuberculosis (TB) endemic country. DESIGN: Multicentre cross-sectional study of 298 HIV patients tested with QuantiFERON®-TB Gold In-Tube (QFT-GIT), T-SPOT®.TB (T-SPOT) and TST. RESULTS: A total of 77/298 (26%) QFT-GIT, 29/117 (25%) T-SPOT and 52/217 (24%) TSTs (≥ 5 mm) were positive. The median CD4 count was 427 cells/l. Three QFT-GIT results but no T-SPOT results were indeterminate. Of 52 TST-positive patients, 34 (65%) were QFT-GIT-positive (median interferon-gamma [IFN-] 4.38 international units [IU]/ml), compared to 16% of the TST-negative patients (median INF- 0.81 IU/ml, P < 0.001). Origin from a TB-endemic country, previous active TB and TB exposure were associated with a positive QFT-GIT (P 0.01). Patients from TB-endemic countries living in Norway for ≥ 10 years had lower odds of a positive QFT-GIT (12%; OR 0.17, 95%CI 0.060.53, P 0.002) than patients with 03 years' residence (49%). CONCLUSION: The prevalence of positive IGRAs in HIV-infected patients was high in this low TB endemic setting. Lower QFT-GIT positivity in long-term residents from TB-endemic countries may reflect a waning of TB-specific immune responses.

Relationship between muscle microstructure, the calpain system, and shear force in bovine longissimus dorsi muscle.

The objective of this study was to examine the occurrence of microstructural changes in aged LM from Norwegian Red cattle, and to investigate how these changes relate to pH decline, calpain and calpastatin activities, and tenderness (Warner-Bratzler shear force; WBSF). Samples of the LM from 403 Norwegian Red dual-purpose bulls were collected over a 4-yr period and analyzed for muscle pH, protease activity, and WBSF. Microstructural analysis of fiber-fiber detachment, muscle fiber-perimysium detachment, contracted muscle fibers, and fractured muscle fibers were performed on a subset of 50 animals. The occurrence of fractured muscle fibers was negatively correlated with WBSF (r = -0.33, P < 0.05) and calpastatin activity (r = -0.51, P < 0.01) and was positively correlated with the ratio of µ-calpain:calpastatin activity (r = 0.66, P < 0.001), strongly indicating that these fractures are important in the development of meat tenderness and that they are a result of calpain-mediated proteolysis. In contrast, detachments between individual muscle fibers and between muscle fibers and the perimysium did not play an important role in determining variation in LM tenderness in these animals. Moreover, both pH decline and what is considered a normal ultimate pH range in beef were positively correlated with calpastatin activity and WBSF and were negatively correlated with fractured muscle fibers. Thus, an accelerated muscle pH decline and a low ultimate pH seem to increase calpain-mediated proteolysis, causing fractures in muscle fibers and thereby giving rise to more tender meat.

Effects of -1.5°C Super-chilling on quality of Atlantic salmon (Salmo salar) pre-rigor Fillets: Cathepsin activity, muscle histology, texture and liquid leakage.

The aim of this study was to evaluate the impact of super-chilling on the quality of Atlantic salmon (Salmo salar) pre-rigor fillets. The fillets were kept for 45min in a super-chilling tunnel at -25°C with an air speed in the tunnel at 2.5m/s, to reach a fillet core temperature of -1.5°C, prior to ice storage in a cold room for 4 weeks. Super-chilling seemed to form intra- and extracellular ice crystals in the upper layer of the fillets and prevent myofibre contraction. Lysosome breakages followed by release of cathepsin B and L during storage and myofibre-myofibre detachments were accelerated in the super-chilled fillets. Super-chilling resulted in higher liquid leakage and increased myofibre breakages in the fillets, while texture values of fillets measured instrumentally were not affected by super-chilling one week after treatment. Optimisation of the super-chilling technique is needed to avoid the formation of ice crystals, which may cause irreversible destruction of the myofibres, in order to obtain high quality products.

Multivariate image analysis of a set of FTIR microspectroscopy images of aged bovine muscle tissue combining image and design information.

In this paper we present an algorithm for analysing sets of FTIR microscopic images of tissue sections. The proposed approach allows one to investigate sets of many FTIR tissue images both with respect to sample information (variation from image to image) and spatial variations of tissues (variation within the image). The algorithm is applied to FTIR microscopy images of beef loin muscles containing myofibre and connective tissue regions. The FTIR microscopy images are taken of sub-samples from five different beef loin muscles that were aged for four different lengths of time. The images were investigated regarding variation due to the ageing length and due to the homogeneity of the connective tissue regions. The presented algorithm consists of the following main elements: (1) pre-processing of the spectra to overcome large quality differences in FTIR spectra and differences due to scatter effects, (2) identification of connective tissue regions in every image, (3) labelling of every connective tissue spectrum with respect to its location in the connective tissue region, and (4) analysis of variations in the FTIR microscopic images in regard to ageing time and pixel position of the spectra in the connective tissue region. Important spectral parameters characterising collagen and proteoglycan structure were determined.

Monitoring of denaturation processes in aged beef loin by Fourier transform infrared microspectroscopy.

We present the results of a Fourier transform infrared (FT-IR) microspectroscopic study using conventional FT-IR microscopy and FT-IR imaging to detect the denaturation process during four different heating temperatures (raw, 45, 60, and 70 degrees C) spatially resolved in bovine cryosections from longissimus dorsi muscle. FT-IR imaging, employing a focal plane array detector, which allowed the simultaneous collection of spectra at 4096 pixels, enabled the investigation of the heat-induced changes in the two major meat constituents, i.e., myofibrillar and connective tissue proteins, spatially resolved. The infrared spectra of both compounds revealed that the major spectral changes involved an increase in beta-sheet and a decrease in alpha-helical structures, which appeared to be much more pronounced for the myofibers than for the connective tissue. These conformational changes could be correlated to the denaturation of the major meat proteins, such as myosin, actin, and collagen.

Polyunsaturated fat and fish oil in diets for growing-finishing pigs: effects on fatty acid composition and meat, fat, and sausage quality.

Forty-eight crossbred growing-finishing pigs were used to study the effects of polyunsaturated fatty acids (PUFA 31%= low and 50%= high) and fish oil (0, 0.2, and 0.4% capelin) diets on fatty acid composition, chemical traits, and sensory properties of the longissimus muscle, fat, and sausages. High levels of PUFA, independent of the level of fish oil, increased oxidation and rancidity for whole muscle (stored at 1 and 8 months at -23 °C) and sausages (TBARS 0.6-1.3). Fish oil at 0.4% in the diet increased TBA values of loin, but did not affect sensory evaluation scores. An interaction between PUFA and fish oil occurred for TBARS values and rancid odour in sausage, where the 0.4% fish oil and high PUFA level showed highest oxidation (TBARS 1.9). Although fish oil and high PUFA levels might contribute to a more healthy meat, their undesirable affects on palatability would limit their use.

Image analysis of particle dispersions in microscopy images of cryo-sectioned sausages.

Two feature extraction methods, the three-dimensional (3-D) local box-counting method and the area distribution method, are presented to describe the fat dispersion pattern on digital microscopy images of cryo-sectioned sausages. Both methods calculate whole arrays of variables for each microscopy image. The 3-D box-counting method calculates scale dependent (local) dimensions. This is in contrast to common fractal methods, which are univariate. Principal component analysis (PCA) was used to show that different sausages yield different fat dispersion patterns. Partial least square regression (PLS) shows that there is a correlation between the variables gained with both methods and the fat content.

Processing of marine foods.

For the Norwegian fish industry, it is an objective to increase the production of value added products in order to improve profitability. This paper will briefly present four areas of important research tasks in this field. To aid in the identification of the species present in a product, we have applied the method called Random Amplification of Polymorphic DNA (RAPD). This technique is used to produce a fingerprint of DNA contained in the sample. The application of DNA typing for species identification in fish products is presented. The nutritional aspects of foods are important. Although the low death rate from coronary heart disease among the Eskimos of Greenland has been suggested to stem in large part from their consumption of fish, one should keep in mind that the daily diet of Eskimos living in the traditional way consists of substantial quantities of meat and fat (blubber) from seals and whales. A recent study as to whether seal and whale oils are more effective than cod liver oil in changing biological parameters that might be important in explaining low incidence of coronary heart disease, asthma and psoriasis among Greenland Eskimos will be presented. Commercial processing of fish must take the development of rigor mortis into consideration since it affects yield and fish flesh quality. Influence of early processing (pre-rigor) on fish quality and yield is also discussed. There are significant differences among fish species in gross chemical composition and morphological structure. Depending on the properties of the flesh and the way it is treated, it may gain or lose water. The relationship between structure and liquid-holding properties of cod and salmon muscle as a function of temperature is presented.

Two-dimensional electrophoretic analyses of cod (Gadus morhua, L.) whole muscle proteins, water-soluble fraction and surimi. Effect of the addition of CaCl2 and MgCl2 during the washing procedure.

Samples from pre- and post-rigor cod mince, surimi (a concentrate of fish myofibrillar proteins obtained after washing and dewatering the fish mince) and water from the first wash in the surimi manufacture, processed with and without the addition of 7.5 mM CaCl2 and 15 mM MgCl2, were analyzed by two-dimensional electrophoresis. The results showed that the main myofibrillar proteins, including myosin, actin and tropomyosin, remained in the surimi. Several other proteins were selectively removed during the washing procedure. Some additional major spots were detected in the two-dimensional gels containing samples of the wash water and surimi processed with the addition of Ca2+ and Mg2+ salts. These spots were either absent or present in minor amounts in the samples of post-rigor cod mince, wash water and surimi processed without Ca2+ and Mg2+ salts and in all the pre-rigor samples. This induced us to suggest that the new additional spots may constitute fragments of proteins originated by increased proteolytic activity during the surimi manufacture upon the addition of the Ca2+ and Mg2+ salts. Two-dimensional electrophoresis has proved to be a valuable tool to quickly and easily assess the effect of different processing conditions on the protein content of the products.

Comparison of myosin isoenzymes present in skeletal and cardiac muscles of the Arctic charr Salvelinus alpinus (L.). Sequential expression of different myosin heavy chains during development of the fast white skeletal muscle.

The expression of myosin isoforms and their subunit composition in the white skeletal body musculature of Arctic charr (Salvelinus alpinus) of different ages (from 77-day embryos until about 5 years old) was studied at the protein level by means of electrophoretic techniques. Myosin from the white muscle displayed three types of light chain during all the developmental stages examined: two myosin light chains type 1 (LC1F) differing in both apparent molecular mass and pI, one myosin light chain type 2 (LC2F) and one myosin light chain type 3 (LC3F). The fastest-migrating form of LC1F seemed to be predominant during the embryonic and eleutheroembryonic periods. The slowest-migrating form of LC1F was predominant in the 5-year-old fish. Between 1 year and 4 years, both types of LC1F were present in similar amounts. Cardiac as well as red muscle myosin from 3-year-old fish had two types of light chain. The myosin light chains from atria and ventriculi were indistinguishable by two-dimensional electrophoresis, but were different from the myosin light chains from red muscle. Neither the light chains from cardiac nor red muscle were coexpressed with the myosin light chains of white muscle at any of the developmental stages examined. Two myosin heavy chain bands were resolved by SDS/glycerol/polyacrylamide gel electrophoresis of the extract from embryos. One of the bands was present in minor amounts. The other, and most abundant, band comigrated with the only band found in the extracts of white muscle myosin from older fish. One-dimensional Staphylococcus aureus V8 protease peptide mapping of these bands revealed some differences during development of the white muscle tentatively interpreted as follows. The myosin heavy chain band present in minor amounts in the embryos may represent an early embryonic form that is replaced by a late embryonic or foetal form in the eleutheroembryos. The foetal myosin heavy chain appears to be present until the resorption of the yolk sack and beginning of the free-swimming stage. A new form of myosin heavy chain, termed neonatal and probably expressed around hatching, is present until about 1 year of age.(ABSTRACT TRUNCATED AT 400 WORDS)

Myosin isoforms in red and white muscles of some marine teleost fishes.

The myosin content from red and white muscles of three marine fish species, saithe (Pollachius virens. L.), haddock (Melanogrammus aeglefinus, L.), both members of the family Gadidae, and capeline (Mallotus villosus, M.) of the family Osmeridae, was analyzed electrophoretically. Analysis of the native myosin by electrophoresis under non-dissociating conditions revealed two isoforms in red muscles, and three or four in white muscles. The white muscles of the two closely related species had a similar pattern of isoforms. Myosin from the slow red muscles had two types of light chain, LC1S and LC2S, and myosin from the fast white muscles three, LC1F, LC2F, and LC3F. The pattern of light chains in both types of muscles was species-dependent. All the light chains from fish myosins were more acidic than those of the rat diaphragm used as standard. One main type of heavy chain was detected in each kind of muscle. In white muscles of saithe there was an extra band, present in minor amounts. The heavy chains from white muscle myosin had lower electrophoretic mobilities than those from red muscle, and the mobilities of all of them were intermediate between those of the heavy chains type IIa and I of rat diaphragm myosin. In our opinion, there are probably more isomyosins in fish muscles than those detected in the present work and their presence is obscured by comigration with the main types.

Intraspecific myosin light chain polymorphism in the white muscle of herring (Clupea harengus harengus, L.).

The myosin contained in white and red muscles of herring (Clupea harengus harengus) was purified, and its subunit composition analyzed by electrophoretic techniques. The only myosin isoform present in red muscles was made up of one type of heavy chain and two types of light chain. The native myosin from white muscles migrated as one wide band. Analysis of the extracts by SDS/glycerol/PAGE from white muscles revealed one main type of heavy chain. Light chains were identified by SDS-PAGE analysis of electrophoretically purified myosin, and two-dimensional electrophoresis of the extracts demonstrated differences in the light chain composition of white and red muscles. Using this methodology, light chain polymorphism was detected in white muscles among members of the same species.

Electrophoretic study of myosin isoforms in white muscles of some teleost fishes.

1. White skeletal muscle myosin of four marine teleost fish species (cod, blue whiting, Norway haddock, and spotted wolf-fish) was analyzed by native, SDS-PAGE, and 2-dimensional electrophoresis. 2. Four types of native myosin were present in cod, blue whiting and Norway haddock. The second fastest migrating form was predominant. 3. Myosin from spotted wolf-fish also resolved into four forms. The fastest migrating form was hardly noticeable. The other three were present in apparently similar amounts. 4. In the myosin from each species there were three types of light chains. The pattern of light chains was species specific. 5. Apparently, there was only one type of heavy chain in myosin from cod, Norway haddock and spotted wolf-fish. One preparation of cod showed an extra band of higher electrophoretic mobility than the main band. In blue whiting we found two bands present in approximately equal amounts.