• Korean Journal of Food Science and Technology
• /
• v.18 no.3
• /
• pp.181-186
• /
• 1986

Myosin were prepared from red muscle and white muscle, and their ATPase activities were compared. Ca-ATPase activity of bovine myosin from red muscle was higher than that of myosin from white muscle, while Ca-ATPase activity of chicken myosin from red muscle differed hardly from that of myosin from whitemuscle. Atso EDTA-ATPase activity of bovine red muscle myosin was higher than that of white muscle myosin ,although EDTA-ATPase activity of chicken myosin from red muscle differed hardly from that of white muscle myosin. When myosins were treated with trypsin, bovine myosin from white muscle was hydrolysed moreeasily than red muscle myosin was. Chicken myosin from red muscle , however, was hydrolysed by trypsin more easily than white muscle myosin was.

• Food Science of Animal Resources
• /
• v.34 no.5
• /
• pp.656-664
• /
• 2014

The purpose of this study was to analyze myosin heavy chain (MHC) isoforms in bovine longissimus thoracis (LT) muscle by liquid chromatography (LC) and mass spectrometry (MS). LT muscles taken from Hanwoo (Korean native cattle) steer (n=3) used to separate myosin bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The peptide queries were obtained from the myosin bands by LC-MS/MS analysis following in-gel digestion with trypsin. A total of 33 and 43 queries were identified as common and unique peptides, respectively, of MHC isoforms (individual ions scores >43 indicate identity or extensive homology, p<0.05). MHC-1 (IIx), -2 (IIa), -4 (IIb), and -7 (slow/I) were identified based on the Mowse score (5118, 3951, 2526, and 2541 for MHC-1, -2, -4, and -7, respectively). However, more analysis is needed to confirm the expression of MHC-4 in bovine LT muscle because any query identified as a unique peptide of MHC-4 was not found. The queries that were identified as unique peptides could be used as peptide markers to confirm MHC-1 (14 queries), -2 (8 queries), and -7 (21 queries) in bovine LT muscle; no query identified as a unique peptide of MHC-4 was found. LC-MS/MS analysis is a useful approach to study MHC isoforms at the protein level.

• Parasites, Hosts and Diseases
• /
• v.33 no.3
• /
• pp.155-164
• /
• 1995

The location of actin and myosin of the several stages of Cwptosporinium parvum was observed. The tissue antigen of C. pcruum was prepared through immunosuppression of IgG mice with Depomedrol . The thin sectioned specimens, which were incubated with the IgG fraction of the rabbit polyclonal antibodies raised against chicken back muscle actin and bovine uterus myosin, were treated with 10 nm gold-conjugated goat anti-rabbit IgG, Electrodense particles were located mainly on the pellicles of all observed developmental stages of the parasites. The number of actin gold particles in the cytoplasm increased when the parasite was dividing actively as in case of meronts. Especially in macrogametocytes, a lot of actin and myosin particles were synthesized and storaged as amilopectin-like bodies. There were many actin gold particles along the microspikes of cytoplasmic membranes in various developmental stages. The actin and myosin observed in this study may play important roles to control the shape of the parasites and movement of cytoplasmic membranes as cvtoskeletal proteins.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
• /
• 2004.05a
• /
• pp.198-201
• /
• 2004

To investigate hydrostatic pressure (HP) effect on myofibrillar protein (Mf) extracted from bovine Semitendinosus muscle, Ca- and Mg-ATPase activities to evaluate denaturation of myosin and actin, and soluble protein contents were observed. In Mf treated with 100 MPa for 5 min was not observed denaturation of myosin and actin. In Mf treated with 200 MPa for 5 min, denaturation of myosin and actin were observed but inactivation rate was low (0.0136 $min^{-1}$). Inactivation rate of myosin and actin was dramatically increased above 300 MPa treatment. However denaturation of myosin and actin was not that critical with duration time. By increasing pressure size, the amount of myosin and actin in soluble protein eluted in 20 mM potassium phosphate buffer (pH 7.0) containing 0.6 M NaCl were decreased. SDS-PAGE of soluble protein released from Mf suspension in 0.1 M NaCl buffer (pH 7.0) showed that low molecular weight proteins (15${\sim}$36 KDa) were released by HP treatment above 200 MPa. From the results, denaturation of myosin and actin, and release of light molecule proteins of Mf were observed by HP treatment over 200 MPa.

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
• /
• 1997.06a
• /
• pp.94-94
• /
• 1997

• Proceedings of the Korean Society for Food Science of Animal Resources Conference
• /
• 1997.11a
• /
• pp.154-154
• /
• 1997

• Preventive Nutrition and Food Science
• /
• v.6 no.2
• /
• pp.91-95
• /
• 2001

Competitive indirect enzyme linked immunosorbent assay (Ci-ELISA) was used to obtain the preliminary data for the detection of irradiated beef. Ci-ELISA was individually formatted with polyclonal antibodies produced from 2 kinds of bovine proteins, myosin and bovine serum albumin (BSA). Beef round, loin and tender loin were vacuum-packaged and subdivided into 3 groups of 1) irradiation; 2) irradiation and chilled at 4$^{\circ}C$ for 7 day; 3) irradiation and frozen at 2$0^{\circ}C$ for 2 months to observe the changes under different storage and/or distribution conditions. Irradiation was performed at 3, 5 and 7 kGy. Protein solutions prepared from the sample were tested by formatted Ci-ELISA. Detected concentrations of myosin and BSA decreased with the increased irradiation dose in all samples with different reduction rates. Myosin was more susceptible to freezing than BSA. Samples irradiated at 5 kGy or above could be differentiated from non-irradiated ones by Ci-ELISA. These results indicate that immunological assay can be used as a detection method for irradiated beef.

• Food Science of Animal Resources
• /
• v.36 no.6
• /
• pp.819-828
• /
• 2016

Muscle fiber characteristics account for meat quality and muscle fibers are mainly classified into three or more types according to their contractile and metabolic properties. However, the majority of previous studies on bovine skeletal muscle are based on myosin ATPase activity. In the present study, the differences in the characteristics of muscle fibers classified by the expression of myosin heavy chain (MHC) among four bovine skeletal muscles such as longissimus thoracis (LT), psoas major (PM), semimembranosus (SM) and semi-tendinosus (ST) and their relationships to beef quality were investigated. MHCs 2x, 2a and slow were identified by LC-MS/MS and IIX, IIA and I fiber types were classified. PM, which had the smallest size and highest density of fibers regardless of type, showed the highest myoglobin content, CIE $L^*$, $a^*$, $b^*$ and sarcomere length (p<0.05), whereas ST with the highest composition of IIX, showed high shear force and low sarcomere length (p<0.05). The correlation coefficients between muscle fiber characteristics and meat quality showed that type IIX is closely related to poor beef quality and that a high density of small-sized fibers is related to redness and tenderness. Therefore, the differences in meat quality between muscles can be explained by the differences in muscle fiber characteristics, and especially, the muscles with good quality are composed of more small-sized fibers regardless of fiber type.

• Korean Journal of Food Science and Technology
• /
• v.30 no.4
• /
• pp.862-870
• /
• 1998

This study shows the application of Ci-ELISA method for monitoring the denaturation of myosin by the frozen treatment in order to differentiate thawed beef from chilled. Hanwoo M.Semitendinosus (n=25) was treated under the two different frozen process as follows; simple frozen treatment (Exp-1) at 4 different temperatures, -10, -20, -50 and $-80^{\circ}C$, respectively, and repeated thawing-refreezing treatment (Exp-2) stored at 4 different temperatures, -10, -20, -50 and $-80^{\circ}C$, respectively. Antibodies (Abs) were produced from rabbits immunized with myosin whole molecule (MWM) isolated from beef round, heavy meromyosin S-1 (S-1) and light meromyosin (LMM) prepared by digestion of MWM. Each immunoglobulin G (IgG) was separated from antiserum. At 6 month storage, IA of anti-MWM IgG for myosin was decreased to 32.67, 32. 23, 51.52 and 34.27% in Exp-1 and to 14.82, 15.61, 25.3 and 23.7% in Exp-2 at -10, -20, -50 and $-80^{\circ}C$, respectively (P<0.05). In Exp-1, the reactivities of anti-LMM IgG were decreased to 25.12, 21.42, 49.05 and 28.96%, and those of Exp-2 were to 11.88, 9.56, 20.63 and 12.64% at -10, -20, -50 and $-80^{\circ}C$, respectively, at 6 times thawing (P<0.05). Conclusively, myosin was denaturated by freezing treatment and LMM or myosin rod part might have suffered from more extreme demage than HMM S-1, and samples at $-50^{\circ}C$ were slightly injured less than others by freezing treatment.

• Asian-Australasian Journal of Animal Sciences
• /
• v.19 no.10
• /
• pp.1496-1502
• /
• 2006

Skeletal muscle contains slow and fast twitch fibers. These skeletal muscle fibers express type I and type II myosin, respectively, and these myosin isoenzymes have different ATPase activity. The aim of this study was to investigate protein profiles of bovine skeletal muscles by proteomic analysis. Fifty seven spots of distinct proteins were excised and characterized. The expression of sixteen spots was differed in longissimus dorsi muscle with a minimal 2-fold change compared to biceps femoris muscle. The majority of differentially expressed proteins belonged to metabolic regulation-related proteins such as glyceraldehyde 3-phosphate dehydrogenase, triosephosphate isomerase and carbonic anhydrase 3. The real time-PCR assay confirmed an increase or induction of specific genes: RGS12TS isoform, GAPDH, triosephosphate isomerase and carbonic anhydrase. These results suggest that the expression of metabolic proteins is under a specific control system in different bovine skeletal muscle. These observations could have significant implications for understanding the physiological regulation of bovine skeletal muscles.