利用AABBDDDD八倍体培育小麦一簇毛麦二体附加系的研究

对普通小麦（Ｔｒｉｔｉｃｕｍ ａｅｓｔｉｖｕｍ）－节节麦（Ａｅｇｉｌｏｐｓ ｓｑｕａｒｒｏｓａ）八倍体（２ｎ＝８ｘ＝５６,ＡＡＢＢＤＤＤＤ）与硬粒小麦（Ｔｒｉｔｉｃｕｍ ｄｕｒｕｍ）－簇毛麦９Ｈａｙｎａｌｄｉａ ｖｉｌｌｏｓａ）六倍体（２ｎ＝６ｘ＝４２,ＡＡＢＢＶＶ）杂交后,将所得七倍体杂种（ＡＡＢＢＤＤＶ）进行连续自交,在Ｆ４代中利用Ｃ－分带鉴定出可能的簇毛麦６Ｖ二体附加系９５－７和２Ｖ二体附加     

多荚草中的新三萜皂甙

从石竹科植物多荚草（Ｐｏｌｙｃａｒｐｏｎ ｐｒｏｓｔｒａｔｕｍ（Ｆｏｒｓｓｋ．）Ａｓｃｈｅｒｓ．ｅｔ Ｓｃｈｗｅｉｎ．ｅｘ Ａｓｃｈｅｒｓ）中分离得到３个新的柴胡皂甙类化合物：ｐｒｏｓｔｒａｔｏｓｉｄｅ Ａ￣Ｃ（１￣３）。它们的结构通过波谱方法分别鉴定为：３－Ｏ－｛β－Ｄ－ｘｙｌｏｐｙｒａｎｏｓｙｌ－（１→２）－β－Ｄ－ｇｌｕｃｏｐｙｒａｎｏｓｙｌ－（１→４）－「β－Ｄ－ｇｌｕｃｏｐｙｒａｎｏｓｙ     

6－Dimethylaminopurine（6－DMAP） Spontaneously Induces Interphase Transition Of Metaphase Mouse Oocytes

６－Ｄｉｍｅｔｈｙｌａｍｉｎｏｐｕｒｉｎｅ（６－ＤＭＡＰ）ＳｐｏｎｔａｎｅｏｕｓｌｙＩｎｄｕｃｅｓＩｎｔｅｒｐｈａｓｅＴｒａｎｓｉｔｉｏｎＯｆＭｅｔａｐｈａｓｅＭｏｕｓｅＯｏｃｙｔｅｓ￥ＳＵＮＱｉｎｇ－ｙｕａｎ（孙青原）;ＧＡＯＳｈａｏ－ｒｏｎｇ（高...     

五种酶组织化学方洁显示大鼠海马微血管的比较

本文对１０例成年Ｗｉｓｔａｒ大鼠海马,应用过氧化物酶二氨基联苯胺（ＤＡＢ）法、碱性磷酸酶（ＡＩＰ）、镁离子激活的三磷酸腺苷酶（Ｍｇ（２＋）－ＡＴＰａｓｅ）、钙离子激活的三磷酸腺昔酶（Ｃａ（２＋）－ＡＴＰａｓｅ）和５’－核苷酸酶（５’－Ｎａｓｅ）等酶组织化学方法显示其微血管,并应用体视学方法测算,比较上述方法显示微血管的效果,结果表明：ＤＡＢ法显示微血管的效果最好,ＡＩＰ法次之,Ｍｇ（２＋）－ＡＴ－Ｐａｓｅ法再次之。大鼠海马微血管Ｃａ（２＋）－ＡＴＰａｓｅ呈弱阳性,５‘－Ｎａｓｅ呈阴性。ＤＡＢ法和Ｍｇ（２＋）－ＡＴＰａｓｅ法分别适宜作微血管长度密度和血管直径的定量分析。     

部分裸子植物叶片总蛋白分析

采用ＳＤＳ－ ＰＡＧＥ 技术, 分析了红豆杉科（Ｔａｘａｃｅａｅ） 植物南方红豆杉（ Ｔａｘｕｓ ｃｈｉｎｅｎｓｉｓｖａｒ－ ｍａｉｒｅｉ （Ｌｅｍｅｅ ｅｔ Ｌｅｖｌ－） Ｃｈｅｎｇ ｅｔ Ｌ－Ｋ－Ｆｕ） 、穗花杉（ Ａｍｅｎｔｏｔａｘｕｓ ａｒｇｏｔａｅｎｉａ （Ｈａｎｃｅ） Ｐｉｌ ｇｅｒ） 、云南穗花杉（ Ａ－ ｙｕｎｎａｎｅｎｓｉｓ Ｌｉ） 、白豆杉（ Ｐｓｅｕｄｏｔａｘｕｓｃｈｉｅｎｉｉ（Ｃｈｅｎｇ） Ｃｈｅｎｇ） 以及三尖杉科（Ｃｅｐｈａｌｏｔａｘａｃｅａｅ） 、植物三尖杉（ Ｃｅｐｈａｌｏｔａｘｕｓ ｆｏｒｔｕｎｅｉ Ｈｏｏｋ－ｆ－） 、粗榧（ Ｃ－ｓｉｎｅｎｓｉｓ （Ｒｅｈｄ－ｅｔＷｉｌｓ－） Ｌｉ） 、海南粗榧（ Ｃ－ｈａｉｎａｎｅｎｓｉｓ Ｌｉ） 、篦子三尖杉（ Ｃ－ｏｌｉｖｅｒｉ Ｍａｓｔ－） 和罗汉松科（Ｐｏｄｏｃａｒｐａｃｅａｅ） 、植 物罗汉松 （ Ｐｏｄｏｃａｒｐｕｓ ｍａｃｒｏｐｈｙｌｌｕｓ （ Ｔｈｕｎｂ－ ） Ｄ－Ｄｏｎ） 、鸡毛 松（ Ｐ－ｉｍｂｒｉｃａｔｕｓ Ｂｌ－） 、竹柏（ Ｐ－ ｎａｇｉ（Ｔｈｕｎｂ－） Ｚｏｌｌ） 、陆均松（ Ｄａｃｒｙｄｉｕｍ ｐｉｅｒｒｅｉ Ｈｉｃｋｅｌ） 共１２ 种植物的叶片蛋白, 在蛋白质水平上采用     

L－NNA和还原型Hb对SHRsp肠系膜动脉内皮依赖性舒张的影响

我们以往的工作证实成年自发高血压大鼠（ＳＨＲ与ＳＨＲｓｐ）肠系膜动脉由乙酰胆碱引起的内皮依赖性舒张（ＥＤＲ）减弱。为进一步探讨ＥＤＲ减弱的机制，本文观察了一氧化氮（ＮＯ）合成酶抑制剂左旋硝基精氨酸（Ｌ－ＮＮＡ）及ＥＤＲＦ灭活剂还原型血红蛋白（ＲＨｂ）对卒中易感型自发高血压大鼠（ＳＨＲｓｐ）与常压对照（ＷＫＹ）大鼠肠系膜动脉ＡＣｈ内皮依赖性舒张（ＥＤＲ）的影响。发现Ｌ－ＮＮＡ（１０（－３）ｍｏｌ／Ｌ）可使ＳＨＲｓｐ弱于ＷＫＹ的ＡＣｈＥＤＲ（１０（－８）－１０（－５）ｍｏｌ／Ｌ）的差异消失，ＲＨｂ（１０（－５）ｍｏｌ／Ｌ）则仅在１０（－７）－１０（－８）ｍｏｌ／ＬＡＣｈ时使ＳＨＲ（ｓｐ）肠系膜动脉ＥＤＲ弱于ＷＫＹ的差异消失。将ＷＫＹ在加入Ｌ－ＮＮＡ后的与加入ＲＨｂ后的ＡＣｈ（１０（－８）－１０（－５）ｍｏｌ／Ｌ）ＥＤＲ进行比较，无显著差异。而将ＳＨＲｓｐ在Ｌ－ＮＮＡ后的与ＲＨｂ后的ＡＣｈ（１０（－８）－１０（－６）ｍｏｌ／Ｌ）ＥＤＲ进行比较，则有显著差异。并且，ＳＨＲｓｐ的有内皮肠系膜动脉条对ＲＨｂ的敏感性与ＷＫＹ接近，对Ｌ－ＮＮＡ的敏感性则低于ＷＫＹ。表明高血压时肠系膜动脉内皮依赖性舒张减弱中，ＥＤＲＦ机制与     

一氧化氮供体增强大鼠记忆及其与脑内ADP-核糖基转移酶的关系

为探讨与学习记忆有关的一氧化氮（ｎｉｔｒｉｃ ｏｘｉｄｅ,ＮＯ）信号转导通路,本文用ＮＯ供体硝普钠（ｓｏｄｉｕｍ ｎｉｔｒｏｐｒｕｓｓｉｄｅ,ＳＮＰ）或同时给予ＡＤＰ－核糖基转移酶（ＡＤＰ－ｒｉｂｏｓｙｌｔｒａｎｓｆｅｒａｓｅ,ＡＤＰＲＴ）抑制剂尼克酰胺（ｎｉｃｏｔｉｎａｍｉｄｅ,ＮＩＣ）侧脑室内流射,观察其对大鼠学习记忆行为的影响,并用高效液相色谱法测定脑内ＡＤＰＲＴ活性。结果表明,ＳＮＰ（０．     

THINOPYRUM BESSARABICUM和THINOPYRUM ELONGATUM的基 …

对２个八倍体Ｃ．Ｓ－Ｔｈｉｎｏｐｙｒｕｍ ｂｅｓｓａｒａｂｉｃｕｍ（ＡＡＢＢＤＤＪＪ,２ｎ＝８ｘ＝５６）和Ｇｏｓｈａｗｋ（ＧＨＫ）－Ｔｈｉｎｏｐｙｒｕｍ ｅｌｏｎｇａｔｕｍ（ＡＡＢＢＤＤＥＥ,２ｎ＝８ｘ＝５６）的根尖细胞染色体进行Ｃ－分带,从中分检出Ｔｈ．ｂｅｓｓａｒａｂｉｃｕｍ和Ｔｈ．ｅｌｏｎｇａｔｕｍ的各自染色体进行核型分析,结果表明：Ｔｈ．ｂｅｓｓａｒａｂｉｃｕｍ和Ｔｈ．ｅｌｏｎｇａｔｕｍ的     

鞭打绣球中的苯丙素甙和环烯醚萜甙

从鞭打绣球（ＨｅｍｉｐｈｒａｇｍａｈｅｔｅｒｏｐｈｙｌｌｕｍＷａｌｌ．）（玄参科）的全草中分离到２个新的苯丙素甙,命名为鞭打绣球甙Ａ和Ｂ（ｈｅｍｉｐｈｒｏｓｉｄｅＡａｎｄＢ）,２个已知的苯丙素甙,ｐｌａｎｔａｍａｊｏｓｉｄｅ和ｐｌａｎｔａｉｎｏｓｉｄｅＤ,以及３个已知的环烯醚萜甙,ｇｌｏｂｕｌａｒｉｃｉｓｉｎ,ｇｌｏｂｕｌａｒｉｎ和ｉｓｏ－ｓｃｒｏｐｈｕｌａｒｉｏｓｉｄｅ．通过化学和光谱分析,鞭打绣球甙Ａ和Ｂ的结构分别鉴定为２－（３－羟基－４－甲氧基苯基）乙基０－β－Ｄ－葡萄吡喃糖基（１→３）－４－Ｏ－反式阿魏醚基－β－Ｄ－葡萄吡喃糖试和２－（３,４－二羟基苯基）乙基Ｏ－［６－Ｏ－乙醚基－β－Ｄ－葡萄吡喃糖基（１→３）］－４－Ｏ－反式咖啡醚基－β－Ｄ－葡萄吡喃糖甙．     

杜氏盐藻细胞质膜氧化还原系统与K^＋吸收

杜氏盐藻（Ｄｕｎａｌｉｅｌｌａ ｓａｌｉｎａ）细胞表面存在氧化ＮＡＤＨ 与还原Ｆｅ（ＣＮ）３－６ 的氧化还原系统（ｒｅｄｏｘｓｙｓｔｅｍ ）。该系统在氧化ＮＡＤＨ 时,抑制Ｋ＋ 的吸收,在还原Ｆｅ（ＣＮ）３－６ 时, 促进Ｋ＋ 的吸收,当ＮＡＤＨ 同时存在时, 促进效应最显著, 高达７３５％ 。外源ＮＡＤＨ 促进藻细胞的氧吸收达１６５％ ,而使胞质ｐＨ 下降; 当ＮＡＤＨ 存在时, Ｆｅ（ＣＮ）３－６ 被快速地还原, 同时藻细胞膜外酸化程度增加。质膜Ｈ＋ －ＡＴＰａｓｅ和氧化还原系统的典型抑制剂都不同程度地抑制Ｋ＋ 吸收; 并且钒酸盐对Ｋ＋ 吸收的抑制可以被加入ＮＡＤＨ 和Ｆｅ（ＣＮ）３－６ 而部分恢复, 表明质膜Ｈ＋ －ＡＴＰａｓｅ和氧化还原系统共同参与了细胞Ｋ＋ 的吸收过程     

SOME FEMALE COORDINATING FACTORS IN AMPHIBIAN FERTILIZATION

The influence of volume and ionic composition of the hydrating media upon the fertility of Bufo arenarum oocyte strings, has been studied with the following results: a) when immersed in equal volumes of ionic and non-ionic media, oocyte strings have been found to become more hydrated in the latter ones; b) oocytes are no longer fertile when hydration is 300–400% of their original weight ( critical hydration ). Fertility is recovered by adding ions or egg water to the medium or by modifying its pH; c) when hydration is beyond 500% of the original string weight ( extensive hydration ) fertility can also be recovered by these treatments, but only after a partial jelly-coat liquefaction by thioglycolate.
Egg water was also studied, and shown to have a buffering capacity between pH 5.5 and 7.0. It seems not to influence acrosomic proteinase release.     

Reexamination of the activation of yeast proteinase B at pH 5: loss of inhibition effect of proteinase B inhibitors

The activation of yeast proteinase B at pH 5 has been suggested to be due to the degradation of a specific inhibitor for the enzyme, IB, by proteinase A. However, we found that when pepstatin, which completely inhibits proteinase A, was included in the pH 5 activation mixture, the same time-dependent activation of proteinase B was observed. Furthermore, proteinase B preparations that were void of proteinase A activity were still activated by incubation at pH 5. We found that the activation of proteinase B at pH 5 was due primarily to the irreversible loss of inhibitory effect of IB, which can be resolved by isoelectrofocusing into four distinct bands with isoelectric points of 4.6, 6.1, 6.8 and 7.6. These four forms of IB showed varying degrees of stability at pH 5, which may explain some of the differing observations reported in the past.     

The isolation and properties of a non-pepsin proteinase from human gastric mucosa.

1. A non-pepsin proteinase, proteinase 2, was successfully isolated free from pepsinogen (by repetitive chromatography on DEAE- and CM-celluloses) from the gastric mucosa of a patient with a duodenal ulcer and the uninvaded mucosa of a patient with a gastric adenocarcinoma. 2. Proteinases 1a and 1b, found in gastric adenocarcinoma, were not found in the gastic mucosa of these patients. 3. Proteinase 2 was shown to have an asymmetrical broad pH-activity curve with a maximum over the pH range 3.0-3.7. 4. Proteolytic activity of proteinase 2 was inhibited by pepstatin; the concentration of pepstatin giving 50% inhibition is of the order of 3nm. 5. Inhibition of proteolytic activity by carbenoxolone and related triterpenoids indicated that at pH 4.0 proteinase 2 possesses structural characteristics relating it to the pepsins and at pH 7.4 to the pepsinogens. 6. The sites of cleavage of the B-chain of oxidized insulin for proteinase 2 at pH 1.7 and pH 3.5 were shown to be similar to those previously established for human pepsin 3 and for the cathepsin E of rabbit bone marrow. 7. The non-pepsin proteinase 2 (cathepsin) of human gastric mucosa has properties more similar to cathepsin E than to the cathepsins D.     

Effect of Culture Medium Composition and pH on the Production of M Protein and Proteinase by Group A Streptococci

The effects of pH, yeast extract, and neopeptone on the production of extracellular proteinase and M protein by group A streptococci were studied with a type 1 strain capable of producing both M protein and proteinase. The strain DS 2036-66 grew moderately well in a semisynthetic broth. M protein was produced without adding peptides to the medium. When added to a medium with 1% glucose, yeast extract (0.1%) was found to stimulate both growth and proteinase formation. Limiting the glucose to 0.25% prevented a drop in pH below 6.7 and prevented proteinase formation. Although less growth occurred with limited glucose, M protein of high specific activity was produced with an actual increase in acid-extractable M protein during the stationary phase of growth. When the medium was buffered at pH 7.85 with tris(hydroxymethyl)aminomethane buffer, 0.5% neopeptone prevented proteinase formation. This was true even in the presence of 1% glucose and 0.1% yeast extract, which resulted in a fall in pH to about 4.8 by 48 hr. Growth was greater than in Todd Hewitt broth, but the specific activity of M protein was considerably less than that found in the medium with glucose limited to 0.25%. Neopeptone was found to have little direct action on crude streptococcal proteinase. Instead, the evidence suggested that neopeptone somehow prevents proteinase elaboration. Yeast extract, on the other hand, appears to stimulate proteinase elaboration. To prevent proteinase formation, neopeptone must be added early, during the logarithmic phase of growth or at the start. In contrast, when yeast extract was added as late as 24 hr, it resulted in the elaboration of extracellular proteinase and in the decline of M protein. When 38 M nontypable strains from the diagnostic laboratory were tested for proteinase activity under conditions similar to those used in the diagnostic laboratory, only six produced much proteinase.     

Granulosa cells regulate intracellular pH of the murine growing oocyte via gap junctions: development of independent homeostasis during oocyte growth

Oocytes grow within ovarian follicles in which the oocyte is coupled to the surrounding granulosa cells by gap junctions. It was previously found that small growing oocytes isolated from juvenile mice and freed of their surrounding granulosa cells (denuded) lacked the ability to regulate their intracellular pH (pH(i)), did not exhibit the pH(i)-regulatory HCO(3)(-)/Cl(-) and Na(+)/H(+) exchange activities found in fully-grown oocytes, and had low pH(i). However, both exchangers became active as oocytes grew near to full size, and, simultaneously, oocyte pH(i) increased by approximately 0.25 pH units. Here, we show that, in the more physiological setting of the intact follicle, oocyte pH(i) is instead maintained at approximately 7.2 throughout oocyte development, and the growing oocyte exhibits HCO(3)(-)/Cl(-) exchange, which it lacks when denuded. This activity in the oocyte requires functional gap junctions, as gap junction inhibitors eliminated HCO(3)(-)/Cl(-) exchange activity from follicle-enclosed growing oocytes and substantially impeded the recovery of the oocyte from an induced alkalosis, implying that oocyte pH(i) may be regulated by pH-regulatory exchangers in granulosa cells via gap junctions. This would require robust HCO(3)(-)/Cl(-) exchange activity in the granulosa cells, which was confirmed using oocytectomized (OOX) cumulus-oocyte complexes. Moreover, in cumulus-oocyte complexes with granulosa cells coupled to fully-grown oocytes, HCO(3)(-)/Cl(-) exchange activity was identical in both compartments and faster than in denuded oocytes. Taken together, these results indicate that growing oocyte pH(i) is controlled by pH-regulatory mechanisms residing in the granulosa cells until the oocyte reaches a developmental stage where it becomes capable of carrying out its own homeostasis.     

The thiol proteinases from the latex of Carica papaya L. I. Fractionation, purification and preliminary characterization

Three thiol proteinases, namely papain, chymopapain and proteinase omega were purified to homogeneity from the latex of Carica papaya L. During the purification procedure, the thiol function of the cysteinyl residues were protected either as mixed disulfides with cysteamine or 2-thiopyridone or as S-sulphenylthiosulfate derivative or after blocking with p-chloromercuribenzoic acid. In marked contrast with earlier publications, chymopapain also was found to be a monothiol proteinase as papain and proteinase omega. The active sites of chymopapain and proteinase omega could not be distinguished from that of papain neither by the analysis of the pH dependence of kcat/Km nor by the examination of the pH dependence of the fluorescence emission spectra.     

An alkaline thiol proteinase in the liver mitochondria of bullfrog, Rana catesbeiana

The mitoplasts were prepared from bullfrog (Rana catesbeiana) liver mitochondria by treatment with digitonin and were then separated into the matrix and inner membrane fractions. The matrix fraction thus obtained was free of lysosomal contaminations and exhibited a distinct proteinase activity. pH dependency of the matrix proteinase activity measured in the presence and absence of iodoacetamide revealed that the matrix contained at least two kinds of proteinase, a major alkaline thiol proteinase having an optimal pH at 8.5 and a minor neutral proteinase having an optimal pH at 7.5. The major matrix proteinase activity was strongly inhibited by leupeptin, chymostatin, antipain and E64-C, an inhibitor of Ca2+-dependent thiol proteinase, while it was scarcely affected by diethylpyrocarbonate. The activity was also inhibited by DTNB and p-chloromercuribenzoate. Addition of hydrocarbon compounds such as ethylene glycol, glycerol, Triton X-100 and poly (ethylene glycol) to the reaction mixture was found to decrease the matrix proteinase activity. Neither cytochrome c nor glutamate dehydrogenase was hydrolyzed when subjected to the matrix proteinase activity in vitro. On the other hand, cytochrome c oxidase was effectively hydrolyzed, and the enzyme associated with the mitochondrial innermembrane fragments was partially hydrolyzed by the major matrix proteinase activity.     

Subcellular distribution of histone-degrading enzyme activities from rat liver.

Chromatin prepared from liver tissue contains a histone-degrading enzyme activity with a pH optimum of 7.5-8.0, whereas chromatin isolated from purified nuclei is devoid of it. The histone-degrading enzyme activity was assayed with radioactively labelled total histones from Ehrlich ascites tumor cells. Among the different subcellular fractions assayed, only lysosomes and mitochondria exhibited histone-degrading enzymes. A pH optimum around 4.0-5.0 was found for the lysosomal fraction, whereas 7.5-8.0 has been found for mitochondria. Binding studies of frozen and thawed lysosomes or mitochondria to proteinase-free chromatin demonstrate that the proteinase associated with chromatin isolated from frozen tissue originates from damaged mitochondria. The protein degradation patterns obtained after acrylamide gel electrophoresis are similar for the chromatin-associated and the mitochondrial proteinase and different from that obtained after incubation with lysosomes. The chromatin-associated proteinase as well as the mitochondrial proteinase are strongly inhibited by 1.0 mM phenylmethanesulfonyl fluoride. Weak inhibition is found for lysosomal proteinases at pH 5. Kallikrein-trypsin inhibitor, however, inhibits lysosomal proteinase activity and has no effect on either chromatin-associated or mitochondrial proteinases. The higher template activity of chromatin isolated from a total homogenate compared to chromatin prepared from nuclei may be due to the presence of this histone-degrading enzyme activity.     

In vitro decondensation of the sperm chromatin in Holothuria tubulosa (sea cucumber) not affecting proteolysis of basic nuclear proteins

Sea urchin and sea star oocyte extracts contain proteolytic activities that are active against sperm basic nuclear proteins (SNBP). This SNBP degradation has been related to the decondensation of sperm chromatin as a possible model to male pronuclei formation. We have studied the presence of this proteolytic activity in Holothuria tubulosa (sea cucumber) and its possible relationship with sperm nuclei decondensation. The mature oocyte extracts from H. tubulosa contain a proteolytic activity to SNBP located in the macromolecular fraction of the egg‐jelly layer. SNBP degradation occurred both on sperm nuclei and on purified SNBP, histones being more easily degraded than protein Ø_o (sperm‐specific protein). SNBP degradation was found to be dependent on concentration, incubation time, presence of Ca²⁺, pH, and this activity could be a serine‐proteinase. Thermal denaturalization of the oocyte extracts (80°C, 10–15 min) inactivates its proteolytic activity on SNBP but does not affect sperm nuclei decondensation. These results would suggest that sperm nuclei decondensation occurs by a mechanism different from SNBP degradation. Thus, the sperm nuclei decondensation occurs by a thermostable factor(s) and the removal of linker SNBP (H1 and protein Ø_o) will be a first condition in the process of sperm chromatin remodeling.     

A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization

A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. A purified 43-kDa proteinase produced by this bacterium showed optimal activity at 50 degrees C and pH 9-10 in 20% NaCl. The activity of the enzyme was enhanced about 2.5-fold by the addition of 20-35% NaCl, and the enzyme was highly stabilized by NaCl. It was found to be a serine proteinase related to either chymotrypsin or subtilisin. It absolutely preferred Ile at the P(2) position of substrates. Thus, the enzyme was found to be a halophilic serine proteinase with unique substrate specificity.