• Archives of Pharmacal Research
• /
• 제9권3호
• /
• pp.157-161
• /
• 1986

Isolated calf thymus nuclei were in vitro methylated with S- adenosy-L-methyl-$^{14}C$ methionine, and the proteins were fractionated according to their solubilities. Histone fraction ($H_{2}SO_{4}$-soluble fraction) contained approximately 60% total radioactivity incorporated, while "residual protein" which was ($H_{2}SO_{4}$-insoluble contained the remaining radio-activity. The "residual protein" was further fractionated into various acidic proteins, which contained very littel of the radioactivity. However, the protein fraction eluted from DEAE-cellulose with 0.5 N NaOH contained the largest amount of radioactivity. This protein was found to be basic in nature by amino analysis.

• Journal of Microbiology
• /
• 제44권4호
• /
• pp.369-374
• /
• 2006

To investigate the mechanism of salt tolerance of gram-positive moderately halophilic bacteria, two-dimensional gel electrophoresis (2-D PAGE) was employed to achieve high resolution maps of proteins of Halobacillus dabanensis $D-8^T$. Approximately 700 spots of proteins were identified from these 2-D PAGE maps. The majority of these proteins had molecular weights between 17.5 and 66 kDa, and most of them were distributed between the isoelectric points (pI) 4.0 and 5.9. Some protein spots were distributed in the more acidic region of the 2-D gel (pI <4.0). This pattern indicated that a number of proteins in the strain $D-8^T$ are acidic. To understand the adaptation mechanisms of moderately halophilic bacteria in response to sudden environmental changes, differential protein profiles of this strain were investigated by 2-D PAGE and $Imagemaster^{TM}$ 2D Platinum software after the cells were subjected to salt shock of 1 to 25% salinity for 5 and 50 min. Analysis showed 59 proteins with an altered level of expression as the result of the exposure to salt shock. Eighteen proteins had increased expression, S proteins were induced, and the expression of 33 proteins was down-regulated. Eight of the up-regulated proteins were identified using MALDI-TOF/MS and MASCOT, and were similar to proteins involved in signal transduction, proteins participating in energy metabolism pathways and proteins involved in stress.

• 한국초지조사료학회지
• /
• 제42권3호
• /
• pp.137-145
• /
• 2022

Aluminum (Al) is one of the major factors adversely affects crop growth and productivity in acidic soils. In this study, the effect of Al on plants in soil was investigated by comparing the protein expression profiles of alfalfa roots exposed to Al stress treatment. Two-week-old alfalfa seedlings were exposed to Al stress treatment at pH 4.0. Total protein was extracted from alfalfa root tissue and analyzed by two-dimensional gel electrophoresis combined with MALDI-TOF/TOF mass spectrometry. A total of 45 proteins differentially expressed in Al stress-treated alfalfa root tissues were identified, of which 28 were up-regulated and 17 were down-regulated. Of the differentially expressed proteins, 7 representative proteins were further confirmed for transcript accumulation by RT-PCR analysis. The identified proteins were involved in several functional categories including disease/defense (24%), energy (22%), protein destination (9%), metabolism (7%), transcription (5%), secondary metabolism (4%), and ambiguous classification (29%). The identification of key candidate genes induced by Al in alfalfa roots will be useful to elucidate the molecular mechanisms of Al stress tolerance in alfalfa plants.

• Archives of Pharmacal Research
• /
• 제27권2호
• /
• pp.206-216
• /
• 2004

The functional role of protein carboxylmethylation (PCM) has not yet been clearly elucidated in the tissue level. The biochemical feature of PCM in porcine spleen was therefore studied by investigating the methyl accepting capacity (MAC) of natural endogenous substrate proteins for protein carboxyl O-methyltransferase (PCMT) in various conditions. Strong acidic and alkaline-conditioned (at pH 11.0) analyses of the MAC indicated that approximately 65％ of total protein methylation seemed to be mediated by spleen PCMT. The hydrolytic kinetics of the PCM products, such as carboxylmethylesters (CMEs), under mild alkaline conditions revealed that there may be three different kinds of CMEs [displaying half-times (T$_{1}$2/) of 1.1 min (82.7％ of total CMEs), 13.9 min (4.6％), and 478.0 min (12.7％)], assuming that the majority of CME is base-labile and may be catalyzed by class I PCMT. In agreement with these results, several natural endogenous substrate proteins (14, 31 and 86 kDa) were identified strikingly by acidic-conditioned electrophoresis, and their MAC was lost upon alkaline conditions. On the other hand, other proteins (23 and 62 kDa) weakly appeared under alkaline conditions, indicating that PCM mediated by class II or III PCMT may be a minor reaction. The MAC of an isolated endogenous substrate protein (23-kDa) was also detected upon acidic-conditioned electrophoresis. Therefore, our date suggest that most spleen PCM may be catalyzed by class I PCMT, which participates in repairing aged proteins.

• Journal of Animal Science and Technology
• /
• 제59권9호
• /
• pp.20.1-20.9
• /
• 2017

Background: Ribonuclease (RNase) is one of the few toxic proteins that are present constantly in snake venoms of all types. However, to date this RNase is still poorly studied in comparison not only with other toxic proteins of snake venom, but also with the enzymes of RNase group. The objective of this paper was to investigate some properties of RNase from venom of Vietnam cobra Naja atra. Methods: Kinetic methods and gel filtration chromatography were used to investigate RNase from venom of Vietnam cobra. Results: RNase from venom of Vietnam cobra Naja atra has some characteristic properties. This RNase is a thermostable enzyme and has high conformational stability. This is the only acidic enzyme of the RNase A superfamily exhibiting a high catalytic activity in the pH range of 1-4, with $pH_{opt}=2.58{\pm}0.35$. Its activity is considerably reduced with increasing ionic strength of reaction mixture. Venom proteins are separated by gel filtration into four peaks with ribonucleolytic activity, which is abnormally distributed among the isoforms: only a small part of the RNase activity is present in fractions of proteins with molecular weights of 12-15 kDa and more than 30 kDa, but most of the enzyme activity is detected in fractions of polypeptides, having molecular weights of less than 9 kDa, that is unexpected. Conclusions: RNase from the venom of Vietnam cobra is a unique member of RNase A superfamily according to its acidic optimum pH ($pH_{opt}=2.58{\pm}0.35$) and extremely low molecular weights of its major isoforms (approximately 8.95 kDa for RNase III and 5.93 kDa for RNase IV).

• Applied Biological Chemistry
• /
• 제41권7호
• /
• pp.505-509
• /
• 1998

Pathogenesis-related proteins중 chitinase를 지황에서 추출하고 분류하였다. 지황 chitinase는 chitin affinity column chromatography로 염기성 및 산성 두개 군으로 분류되었으며 native PAGE gel상 효소활성을 조사한 결과 이동도가 작은 염기성 chitinase는 pH 2.9의 산성추출 조건에서, 이동도가 큰 산성은 pH 8.8의 염기성추출 조건에서 상대적으로 많이 추출되었다. 지황에는 염기성 3개, 산성 4개등 총 7개의 chitinase isoform이 존재하며 이들의 분자량은 $28{\sim}32\;kD$내외이고 지상부와 달리 뿌리에는 주로 염기성 chitinase만 검출되어 일부 산성효소는 조직 특이적으로 발현될 가능성을 보여주고 있다.

• Journal of Oral Medicine and Pain
• /
• 제17권2호
• /
• pp.99-108
• /
• 1992

The purpose of this study was to evaluate the polymorphosms in parotid salivary proteins of the patients with diabetes mellitus. Saliva from the parotid glands was collected from 94 healthy Korean adults who were live in Kwang-ju and from 33 diabetes mellitus patients who had more than 140mg/dl of fastingblood sugar for one week. Diabetes mellitus patient group was subdivided to insulin dependent diatetes mellitus (IDDM) and non-insulin dependent diabetes mellitus (NIDDM). In the saliva collected from the parotid glands, parotid acidic protein(Pa), proline-rich protein(Pr) and double band protein(Db) were analyzed to evaluate the distribution of phenotype using alkaline slab polyacrylamide gel electrophoresis. The results were as follows : 1. The parotid acidic protein (Pa) was found more frequently in the diabetes mellitus patient group than in the control group, but the difference was not statistically significant. 2. The Pr(1-2) type was found more frequently in the control group, but the Pr(1-1) and Pr(2-2) type were found more freqnently in the diabetes mellitus patient group and the difference of phenotypic distribution was statistically significant between the two groups. (p<0.05) 3. The parotid acidic protein(Pa) and Pr(1-2) type were found more frequently in the noninsulin dependent diabetes mellitus (NIDDM) patients than in the insulin dependent diabetes mellitus patients, though the difference was not statistically significant.

• BMB Reports
• /
• 제57권9호
• /
• pp.400-416
• /
• 2024

Matricellular proteins are integral non-structural components of the extracellular matrix. They serve as essential modulators of immunometabolism and tissue homeostasis, playing critical roles in physiological and pathological conditions. These extracellular matrix proteins including thrombospondins, osteopontin, tenascins, the secreted protein acidic and rich in cysteine (SPARC) family, the Cyr61, CTGF, NOV (CCN) family, and fibulins have multi-faceted functions in regulating immune cell functions, metabolic pathways, and tissue homeostasis. They are involved in immune-metabolic regulation and influence processes such as insulin signaling, adipogenesis, lipid metabolism, and immune cell function, playing significant roles in metabolic disorders such as obesity and diabetes. Furthermore, their modulation of tissue homeostasis processes including cellular adhesion, differentiation, migration, repair, and regeneration is instrumental for maintaining tissue integrity and function. The importance of these proteins in maintaining physiological equilibrium is underscored by the fact that alterations in their expression or function often coincide with disease manifestation. This review contributes to our growing understanding of these proteins, their mechanisms, and their potential therapeutic applications.

• Applied Biological Chemistry
• /
• 제31권4호
• /
• pp.361-370
• /
• 1988

유청 및 대두 단백질의 상호작용을 규명하기 위하여 두 단백질용액 및 1 : 1 혼합용액에 대한 겔투과크로마토그래피와 전기영동에 의하여 열처리 중 조성단백질의 변화 및 상호작용에 관여한 조성단백질을 조사하였다. 크로마토그래피 결과 $80^{\circ}C$ 이상에서 열처리할 경우, 대두단백질 및 혼합물에서 저분자량의 단백질과 고분자량의 응집물이 증가한 것으로 나타났는데, 이는 열처리에 의하여 대두의 11S globulin이 subunit로 해리되고, 이것이 thiol기, disulfide bond 등을 함유한 유청단백질과 가용성 응질물을 형성하기 때문으로 생각되었다. 전기영동에 의하여, 가열시 유청조성단백질 중의 ${\beta}-Lactoglobulin$, ${\alpha}-Lactalbumin$ 및 proteose-peptone 3이 대두단백질과 상호작용을 일으키는 것으로 나타났다. 그리고 용액의 염환경에 따라 Bovine Serum Albumin, Immunoglobulin G(H) 및 Lactoferrin도 상호작용을 일으킬 수 있으며, 대두조성단백질 중의 11S globulin의 basic subunit와 acidic subunit, 7S globulin의 ${\alpha}'$ subunit가 유청단백질과 상호작용을 일으킬 수 있음을 추측할 수 있었다.

• Journal of Oral Medicine and Pain
• /
• 제19권2호
• /
• pp.233-244
• /
• 1994

The purpose of this study was to evaluate the gene frequency in parotid salivary proteins according to salivary blood components and salivary blood types. Parotid and whole saliva were collected from 160 healthy Korean adults (from 20 years of age to 43). They were divided by blood type(Q,B, AB,O type). Each group contained 40 adults respectively. They were tested to the salivary secretory blood components and parotid acidic protein(Pa), proline-rich protein(Pr) and double band protein(Db) were analyzed to evaluate the distribution of phenotype using alkaline slab polyacrylamide gel electrophoresis. Results were as follows : 1. In parotid saliva, the salivary blood substances were not found. In whole saliva, secretory type was 21.9% and non-secretory type was 78.1%. : In A type blood group, secretory type 87.5% and non-secretory type 12.5%. In B type blood group, secretory type 82.5% and non-secretory type 17.5%. In AB type blood group, secretory type 85% and non-secretory type 15%. In O type blood group, secretory type 57.5% and non-secretory type 42.5%. 2. The gene frequency of parotid acidic protein(Pa) were Pa+=0.160, Pa-=0.840 and proline-rich protein(Pr) were Pr1=0.781, Pr2=0.219 and double-band protein(Db) were Db+=0.019, Db-=0.981. 3. The difference between phenotype of Pa, Pr, Db proteins and salivary secretory blood components was not statistically significant. (P>0.05) 4. The difference between phenotype of Pa, Pr, Db proteins and blood types was not statistically significant.(P>0.05)