• BMB Reports
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• v.33 no.6
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• pp.510-513
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• 2000

Boar sperminogen was purified from the acid extracts of the washed epididymal spermatozoa by gel filtration through a Sephadex G-100 column, followed by preparative SDS-PAGE. The 32 kDa sperminogen band was sliced out from the preparative SDS-PAGE and 32 kDa sperminogen was eluted from the gel matrix. The purified 32 kDa sperminogen was subjected to amino acid composition analysis. The amino acid composition of the 32 kDa boar sperminogen showed significant differences from that of either boar proacrosin or ${\beta}-acrosin$, which signifies that 32 kDa sperminogen might not be a breakdown product of proacrosin-acrosin system and that the 32 kDa sperminogen is a different protein from proacrosin-acrosin system.

• Proceedings of the KSAR Conference
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• 2001.03a
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• pp.86-86
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• 2001

The aims of this work were to determine the acrosin activity and to evaluate the structural and functional integrity of AS boar spermatozoa. The acrosin activity of spermatozoa were 5.40, 4.10 and 3.40 mIU/10$^{6}$ sperm in raw, extended and frozen semen respectively , which differed significantly each other (P<0.05). After the raw and extended semen were exposured to cold and thermal shock, the acrosin activities of spermatozoa in the raw semen were 5.39, 5.21 and 5.29 mIU/10$^{6}$ sperm for control (non-shock), cold shock and thermal shock, and those of extended semen were 4.21, 3.98 and 4.00 mIU/10$^{6}$ sperm. This value among treatments did not differ significantly. The acrosin activities of spermatozoa in the extended and stored semen were 3.27, 3.52, 3.46 and 3.23 mIU/10/suup 6/ sperm, while hypo-osmotic test(HOST) values were 56.5%, 64.7%, 66.0% and 56.0%, following 4 days storage at 4$^{\circ}C$, 17$^{\circ}C$ , $25^{\circ}C$ and 37$^{\circ}C$, respectively. The results at 17$^{\circ}C$ and $25^{\circ}C$ appeared to be best compared with the other storage temperatures.

• BMB Reports
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• v.30 no.6
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• pp.448-452
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• 1997

Polyclonal antibody of the boar sperminogen was used to characterize the boar sperm proteinase sperminogen. Boar sperminogen was purified from the acid extracts of the washed epididymal spermatozoa by gel filtration through a Sephadex G-100 column. followed by preparative SDS-PAGE. The sperminogen band was sliced out and was eluted from the gel matrix. The purified sperminogen was used to produce the polyclonal antibody of the boar sperminogen. When characterized on a Western blot, the final preparation of sperminogen appeared as a homogenous protein with a molecular weight of 32 kDa. The relative migration of sperminogen was distinctly different from the major components of the proacrosin-acrosin system as well as all the observable proacrosin activation by-products detected on the Western blot. The sperminogen antibody, however. cross-reacted with the proacrosin-acrosin system.

• Proceedings of the KSAR Conference
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• 2001.03a
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• pp.10-10
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• 2001

본 연구는 정자의 기능검사와 체외수정을 실시하여 수정능력과 수태율의 예측을 위한 이들간의 상관관계를 알아보기 위하여 AI 중인 8두의 종모돈을 가지고 시도되었다. 정자의 기능검사로서 첨체상태는 spermac stain을 이용하여 관찰하였고 정자원형질막의 온전성(integrity) 검사로는 hypo-osmotic test(HOST)를 실시하였다. 그리고 정자의 첨체효소인 acrosin activity를 측정하였다. 체외수정율은 체외성숙 난포란과 실시하였다. 8마리 종모돈의 첨체형태의 정상비율은 처리전 64.7-81.9%, 처리후 21.8~48.1%로 개체간의 유의성이 있었다. Acrosin activity는 처리전 3.70-4.57 mIU/$10^{6}$ 정자, 처리후 3.23~5.53 mIU/$10^{6}$ 정자였으며 처리전 개체에서만 유의성이 있었다. HOST는 처리전 26.5~54.5%, 처리후 20.2~50.0%로서 처리전후간의 차이는 없었지만 개체간의 유의차는 있었다. 체외수정율의 범위는 61.6~8l% 였고 6일 후 배발달율(배반포율)은 11~22%로 개체간의 유의성이 있었다. Spearman ranking correlation에서 체외수정율은 첨체상태검사와는 0.45, HOST와는 0.43로서 유의성이 인정되지 않았다. 또한 수태율은 첨체상태검사와 0.89, acrosin activity와 0.86, HOST와 0.86, 체외수정과 0.51로서 유의적으로 높은 상관관계를 나타내었다. 본 결과에서 종모돈의 기능검사와 체외수정결과로 개체간의 수정능력의 차이를 알 수 있었으나 수정란의 발달율이나 수태율을 예측할 수 있을 만큼의 상관성은 얻지 못했다. 정자검사에 있어서 일반성상 검사외에 정자기능 검사의 추가 실시가 종모돈 정자의 정확한 수정능력을 예측하는데 필요할 것이다.llus kawachii등으로 담금하여 제조한 술 시료 11종류를 대상으로 하여 쓴맛, 미묘한 맛, 떫은 맛, 신맛, 좋은 맛의 정도를 5단계로 나누어 관능검사를 실시한 다음 자료를 Duncan's multiple range test로 분석한 결과 전체적으로 좋은 맛에 대한 기호도는 Aspergillus sp. SH-607 시료와 Aspergillus sp. SH-412, Rhizopus sp. SH-606, Aspergillus sp. SH-613, Rhizopus sp. SH-654, Aspergillus sp. SH-696 Aspergillus kawachii 시료가 유의성 있게 좋은 맛을 나타내 기호도가 높았으며 맛과 기호도가 가장 좋았던 것은 Aspergillus sp. SH-607 시료로 나타났다.\varepsilon}}$는 268.20 $m^2$/day, $T_{ηη}$는 28.75 $m^2$/day이고 주 텐서방향은 N7.55$^{\circ}$E이며 BH-5호공에서의 $T_{{\varepsilon}{\varepsilon}}$는 168.40 $m^2$/day, $T_{ηη}$는 66.80 $m^2$/day이고 주 텐서방향은 N76.59$^{\circ}$E로 나타났다. 이처럼 연구지역에서의 각각의 공에 대한 투수량계수텐서는 서로 다르게 나타났으며 이에 따른 주 텐서방향도 서로 다름을 알 수 있다.. Targeting a 10% recycling rate for municipal waste in 2001. EPA plans to research and develop new recycling techniques, expand t

• Clinical and Experimental Reproductive Medicine
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• v.25 no.1
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• pp.43-50
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• 1998

This study was performed to determine the effects of nitric oxide on human sperm cell function. Semen samples were obtained from normal healthy volunteers. Motile spermatozoas collected by swim-up method were incubated up to 24 hours in Ham's F-10 medium supplemented with a various concentration of sodium nitroprusside (nitric oxide releasing agent). Sperm motility, hyperactivation, acrosome reaction rate, and acrosin activity were determined. The results are as follows; 1. 1mM of SNP resulted in a significant decrease in sperm motility ($44.8%{\pm}8.9%:78.1%{\pm}6.3%$, and hyperactivation $(10.4%{\pm}6.4%:47.7%:{\pm}9.5%)$ after incubation for 3 hours compared with the control group (Ham's F-10 alone), but had no effect on acrosome reaction. 2. At $100{\mu}M$ SNP, sperm motility was reduced after incubation for 6 hours $(54.8%{\pm}3.2%)$ compared with that of the control group $(82.7%{\pm}8.9%)$, but hyperactivation and acrosome reaction were not affected. 3. However, a lower concentration (less than $10{\mu}M$) of SNP had no effect on sperm motility and hyperactivation for 8 hours of incubation but significantly decreased them when incubation periods were increased up to 24 hours compared with the control group. On the other hand, $1{\mu}M$ and $10{\mu}M$ SNP significantly increased the acrosome reaction rate in both acrosomal status ($17.3%{\pm}5.2%$, $23.5%{\pm}4.7%$, respectively) and acrosin activity ($34.3{\mu}IU{\pm}10.5{\mu}IU,\;45.6{\mu}IU{\pm}5.6{\mu}IU$, respectively) as compared with the control group $(7.0%{\pm}4.0%,\;9.5{\mu}IU{\pm}3.4{\mu}IU)$. These results indicate that SNP, NO releasing agent, has a dose-dependent effects on the sperm cell function. Therefore it may positively affect the fertilization by promoting acrosomal reaction at a lower concentration (less than $10{\mu}M$).

• Clinical and Experimental Reproductive Medicine
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• v.18 no.1
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• pp.101-105
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• 1991

Although many therapies have been advocated in the treatment of idiopathic male infertility, the results of treatment are poor. This probably seems to be due to a lack of one or more proteins constituting the key structures of the spermatozoa. We evaluated the functional structures of the spermatozoa in 11 infertile patients whose semen showed severe oligoasthenozoospermia with immunochemical method and found a case with spermatozoa lacking acrosin. Evaluation of the spermatozoal defect with immunochemical method is desirable in patients with severe oligoasthenozoospermia, especially in cases unresponsive to medical therapy.

• Animal cells and systems
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• v.5 no.3
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• pp.199-203
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• 2001

Sperminogen was purified from the acid extracts of boar spermatozoa and partial peptide sequence of the 34-36 kd sperminogen was determined. Acid extracts of boar spermatozoa was gel-filtered through Sephadex G-75, and the 34-36 kd sperminogen was purified by preparative SDS-PAGE. The sperminogen bands were sliced out, and 34-36 kd sperminogen were eluted from the gel fragments and was subjected to peptide sequencing. Since the amino termini were blocked for Edman degradation method, internal amino acid sequences of the eluted 34-36 kd sperminogen were obtained from CNBr-digested peptides of sperminogen. Among several bands resolved on tricine SDS-PAGE, 14, 22 and 26 kd peptides were subjected to peptide sequencing. The ana1yzed amino acid sequences of the 26 and 22 kd peptides showed high homologies with that of the zona pellucida binding protein, Sp38, and the analyzed amino acid sequence of the 14 kd peptide showed neither sequence homology nor similarity with any known proteins.

• Clinical and Experimental Reproductive Medicine
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• v.10 no.1
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• pp.7-24
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• 1983

On the basis of the semen analysis in 66 subjects, they were divided into six different groups: Group I consisted of 16 normal subjects with sperm counts of over 40 ${\times}10^6$/ml and motility of over 40 percent, Group II, 7 subjects with normal sperm counts, but motility of under 40 percent, Group III, 15 oligospermic patients with under 40 ${\times}10^6$/ml, Group IV 14 azoospermic patients, Group V, 10 patients with vasectomy and Group VI, 4 abnormal patients with 2 cases of hypoplastic testis, 1 case of Klinefelter's syndrome and 1 case of testis tumor. After seperation of semen into sperm and seminal plasma by centrifugation, the protein contents and the activities of hyaluronidase, ${\beta}$-N acetylglucosaminidase, ${\beta}$-glucuronidase, arylsulfatase, acrosin and azocoll proteinase in seminal plasma were measured. Vasectomy group has 30 percent less of total protein than normal group. For the comparison of enzyme activities of seminal plasma, it could be assumed that the enzymes in seminal plasma were not contaminated with the enzymes of spermatozoa by testing the enzymes of the seminal plasma from the vasectomy and azoospermic groups. It had been reported that hyaluronidase was only released from spermatozoa, however, the result obtained in this investigation showed that azoospermic and vasectomy group had high specific activities of hyaluronidase. The results indicated that hyaluronidase was not only from the testis but also from the male accessory sexual glands. Oligospermic group (Group III) showed the lowest total activity of hyaluronidase among them. The specific activities of ${\beta}$ -N-acetylglucosaminidase was high in oligospermic group (Group III) and low in vasectomy group (Group V). These results were contradictory with the pattern of hyaluronidase activities. This indicated that the spermatozoa which were stayed in epididymis would increase the activity of this enzyme. The specific activity of ${\beta}$ - glucuronidase was low in oligospermic and vasectomy groups. Group VI including testis tumor had remarkably high arylsulfatase activity. Arylsulfatase, a typical lysosomal enzyme, has been known to be released unusually large amounts from certain tumor cells. Arylsulfatase was also released with high activities from azoospermic and vascetomy group. This result indicated that this enzyme was also released from the sources other than testis. Acrosin, a proteolytic enzyme locating in the sperm acrosome, was not found throughout all the samples of seminal plasma. The activities of azocoll proteinase, a non-specific neutral proteinase was nearly identical in all the groups. This enzyme must have been released from the sources other than testis.

• Korean Journal of Oriental Medicine
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• v.12 no.3 s.18
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• pp.131-141
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• 2006

Hominis Placenta has a broad array of clinical applications in Korean medicine, including treatment of inflammatory conditions such as rheumatoid arthritis. The purpose of this study is to explore the global gene expression profiles in human RAW 264.7 cell lines treated with Hominis Placenta herbal-acupuncture solution (HPHAS) using microarray analysis. The RAW 264.7 cells were treated with lipopolysaccharide (LPS), HPHAS, or both. Of the 8,170 genes profiled in this study, with a cut-off level of two-fold change in the expression, 72 genes (CTD1, regulating synaptic membrane exocytosis 2, etc.) were upregulated and 135 genes(splicing factor, arginine/serine-rich 1, actinin, alpha 1, etc.) downregulated following LPS treatment. One gene (acrosin) was upregulated and 12 genes (phospholipase A2, group IB, neurofilament, heavy polypeptide 200kDa, etc.) were downregulated following HPHAS treatment. Eleven genes (RAB27A, member RAS oncogene family, eosinophil peroxidase, etc.) were upregulated and 16 genes (V-maf musculoaponeurotic fibrosarcoma oncogene homolog G (avian), RW1 protein, etc.) were downregulated following co-stimulation of HPHAS and LPS. It is thought that microarrays will play an ever-growing role in the advance of our understanding of the pharmacological actions of HPHAS in the treatment of arthritis. Further studies, however, are required to concretely prove the effectiveness of HPHAS.